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Chapter 4 : Reversal of Base Damage Caused by UV Radiation

Authors: C. Friedberg Errol1, C. Walker Graham2, Siede Wolfram3, D. Wood Richard4, A. Schultz Roger5, Ellenberger Tom6
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Affiliations: 1: Department of Pathology, University of Texas Southwestern Medical Center, Dallas, Texas; 2: Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts; 3: Department of Cell Biology and Genetics, University of North Texas Health Science Center, Fort Worth, Texas; 4: Hillman Cancer Center, University of Pittsburgh, Pittsburgh, Pennsylvania; 5: Department of Pathology, University of Texas Southwestern Medical Center, Dallas, Texas; 6: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts
Content Type: Reference
Publication Year: 2006

Category: Microbial Genetics and Molecular Biology

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Abstract:

This chapter considers several examples of the direct reversal of DNA damage, all of which are catalyzed by single polypeptide enzymes. Both cyclobutane pyrimidine dimers (CPD) and (6-4) pyrimidine-pyrimidone photoproducts [(6-4)PP] constitute quantitatively and qualitatively important sources of base damage following the exposure of cells to UV radiation at wavelengths near the absorption maximum of DNA. The chapter discusses a specific DNA repair mode called enzymatic photoreactivation (EPR), or simply photoreactivation. Enzymes that catalyze EPR of CPD in DNA are referred to as pyrimidine dimer-DNA photolyases (PD-DNA photolyase), pyrimidine dimerdeoxyribodipyrimidine photolyases, or pyrimidine dimerphotoreactivating enzymes. The prefix “pyrimidine dimer” is added to distinguish these enzymes from those that catalyze the repair of (6-4)PP by an essentially identical mechanism. These are called (6-4) photoproduct-DNA photolyases ((6-4)PP-DNA photolyase). The chapter describes distribution, properties, structural studies and mechanism of action of PD-DNA photolyase. It also describes PD-DNA photolyase from other organisms and its therapeutic use for protection against sunlight. Next, it explains mechanism of action and C-terminal region of (6-4)PP-DNA photolyase. In addition, the phylogenetic relationships between PD-DNA photolyases, (6-4)PP-DNA photolyases, and blue-light receptor proteins have been suggested, and the following primary subfamilies of proteins have been defined: (i) PD-DNA photolyase proteins; (ii) plant CRY and plant and animal (6-4)PP-DNA photolyase proteins; and (iii) animal CRY proteins. Other covered topics are repair of thymine dimers by a deoxyribozyme, photoreactivation of RNA, and reversal of spore photoproduct in DNA.

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Reversal of Base Damage Caused by UV Radiation
Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–1
Schematic illustration of the enzyme-catalyzed monomerization of pyrimidine dimers by DNA photolyase (photoreactivating enzyme), an example of DNA repair by the reversal of base damage. The gold square and triangle represent the two noncovalently bound chromophores required for catalytic activity in all DNA photolyases.
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Figure 4–1

Schematic illustration of the enzyme-catalyzed monomerization of pyrimidine dimers by DNA photolyase (photoreactivating enzyme), an example of DNA repair by the reversal of base damage. The gold square and triangle represent the two noncovalently bound chromophores required for catalytic activity in all DNA photolyases.

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–2
Schematic illustration of the measurement of thymine-containing pyrimidine dimers (T<>T, T <>C, C<>C) in DNA. DNA radiolabeled in thymine (T) is exposed to UV radiation to produce pyrimidine dimers, some of which contain radiolabeled thymine. The DNA is hydrolyzed in strong acid at high temperature, resulting in the preservation of structurally intact radiolabeled thymine monomers and radiolabeled thymine-containing pyrimidine dimers. These species can be resolved, and the number of thymine-containing pyrimidine dimers can be quantitated by thin-layer chromatography. The thymine dimer content of the DNA is then expressed as the fraction of the total radioactivity in thymine present as thymine-containing pyrimidine dimers (see Fig. 4–3 ).
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Figure 4–2

Schematic illustration of the measurement of thymine-containing pyrimidine dimers (T<>T, T <>C, C<>C) in DNA. DNA radiolabeled in thymine (T) is exposed to UV radiation to produce pyrimidine dimers, some of which contain radiolabeled thymine. The DNA is hydrolyzed in strong acid at high temperature, resulting in the preservation of structurally intact radiolabeled thymine monomers and radiolabeled thymine-containing pyrimidine dimers. These species can be resolved, and the number of thymine-containing pyrimidine dimers can be quantitated by thin-layer chromatography. The thymine dimer content of the DNA is then expressed as the fraction of the total radioactivity in thymine present as thymine-containing pyrimidine dimers (see Fig. 4–3 ).

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–3
Loss of thymine-containing pyrimidine dimers from acid-precipitable DNA after incubation of UV-irradiated DNA with DNA photolyase in the presence of photoreactivating light.
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Figure 4–3

Loss of thymine-containing pyrimidine dimers from acid-precipitable DNA after incubation of UV-irradiated DNA with DNA photolyase in the presence of photoreactivating light.

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–4
Structures of chromophores found in pyrimidine dimer-DNA photolyases. The folate class of DNA photolyases contains FADH and 5,10-MTHF with appended polyglutamate residues. The deazaflavin class of DNA photolyases contains FADH and 8-HDF. (Adapted from reference .)
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Figure 4–4

Structures of chromophores found in pyrimidine dimer-DNA photolyases. The folate class of DNA photolyases contains FADH and 5,10-MTHF with appended polyglutamate residues. The deazaflavin class of DNA photolyases contains FADH and 8-HDF. (Adapted from reference .)

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–5
The absorption (ε) and absolute-action (εΦ) spectra of DNA photolyases of the folate class (E. DNA photolyase) and deazaflavin class DNA photolyase). The gold lines show the spectra of the holoenzymes. The black lines are the spectra of the enzyme with just FADH. Hence, the shape and maximum wavelengths of the absorption and action spectra in the range of 300- to 500-nm light are determined primarily by the second chromophore (5,10-MTHF in the folate class and 8-HDF in the deazaflavin class). (Adapted from reference .)
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Figure 4–5

The absorption (ε) and absolute-action (εΦ) spectra of DNA photolyases of the folate class (E. DNA photolyase) and deazaflavin class DNA photolyase). The gold lines show the spectra of the holoenzymes. The black lines are the spectra of the enzyme with just FADH. Hence, the shape and maximum wavelengths of the absorption and action spectra in the range of 300- to 500-nm light are determined primarily by the second chromophore (5,10-MTHF in the folate class and 8-HDF in the deazaflavin class). (Adapted from reference .)

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–6
Kinetics of the incision of UV-irradiated DNA by the UvrABC endonuclease for nucleotide excision repair in the presence or absence of PD-DNA photolyase. (Adapted from reference .)
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Figure 4–6

Kinetics of the incision of UV-irradiated DNA by the UvrABC endonuclease for nucleotide excision repair in the presence or absence of PD-DNA photolyase. (Adapted from reference .)

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–7
Summary of the mechanism of enzymatic photoreactivation by PD-DNA photolyases. 1, A blue-light photon is absorbed by the MTHF photoantenna. 2, The excitation energy is then transferred to the active-site flavin (FADH−). 3, The excited flavin contributes an electron to a CPD in DNA. 4, Electronic rearrangements restore the thymine bases to their native state, and the electron is transferred back to the ground-state neutral flavin radical. (Adapted from reference .)
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Figure 4–7

Summary of the mechanism of enzymatic photoreactivation by PD-DNA photolyases. 1, A blue-light photon is absorbed by the MTHF photoantenna. 2, The excitation energy is then transferred to the active-site flavin (FADH−). 3, The excited flavin contributes an electron to a CPD in DNA. 4, Electronic rearrangements restore the thymine bases to their native state, and the electron is transferred back to the ground-state neutral flavin radical. (Adapted from reference .)

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–8
Ribbon diagram of PD-DNA photolyase protein. Conserved residues flanking the FAD chromophore are shown. The second chromophore, the MTFH photoantenna, is located on the back side of the protein.
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Figure 4–8

Ribbon diagram of PD-DNA photolyase protein. Conserved residues flanking the FAD chromophore are shown. The second chromophore, the MTFH photoantenna, is located on the back side of the protein.

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–9
Solvent-accessible surface of the PD-DNA photolyase from the thermophile The surface is colored to show the positive electrostatic potential (gold) surrounding the pocket that binds thymine. The thymine base binds specifically to a pocket adjacent to the FAD cofactor (see Fig. 4–8 ). It is proposed that base flipping would expose a CPD in DNA and facilitate binding in this pocket.
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Figure 4–9

Solvent-accessible surface of the PD-DNA photolyase from the thermophile The surface is colored to show the positive electrostatic potential (gold) surrounding the pocket that binds thymine. The thymine base binds specifically to a pocket adjacent to the FAD cofactor (see Fig. 4–8 ). It is proposed that base flipping would expose a CPD in DNA and facilitate binding in this pocket.

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–10
The PD-DNA photolyase was crystallized in complex with DNA containing a cyclobutane thymine photodimer ( ). The enzyme reactivated the DNA during exposure of the crystals to an intense X-ray beam, resulting in a crystal structure of the enzyme-product complex with unlinked 5’ and 3’ thymines. The thymines are flipped into a pocket in the enzyme-active site, approximately 7 Å from the FADH electron donor. The light-harvesting antenna 8-HDF is positioned near the N-terminal subdomain in a position analogous to the methylene tetrahydrofolate antenna of PD-DNA photolyase (see Fig. 4–8 ). (Adapted from reference .)
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Figure 4–10

The PD-DNA photolyase was crystallized in complex with DNA containing a cyclobutane thymine photodimer ( ). The enzyme reactivated the DNA during exposure of the crystals to an intense X-ray beam, resulting in a crystal structure of the enzyme-product complex with unlinked 5’ and 3’ thymines. The thymines are flipped into a pocket in the enzyme-active site, approximately 7 Å from the FADH electron donor. The light-harvesting antenna 8-HDF is positioned near the N-terminal subdomain in a position analogous to the methylene tetrahydrofolate antenna of PD-DNA photolyase (see Fig. 4–8 ). (Adapted from reference .)

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–11
Schematic diagram of the yeast promoter. The nucleotide sequences of the indicated regulatory elements UES, UAS, and URS are shown. Arrows above sequences indicate palindromes. The white bar under the URS sequence is the binding site for Rph1 protein. Numbering at the top of the figure is relative to the first ATG translational start codon in the coding sequence. (Adapted from reference .)
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Figure 4–11

Schematic diagram of the yeast promoter. The nucleotide sequences of the indicated regulatory elements UES, UAS, and URS are shown. Arrows above sequences indicate palindromes. The white bar under the URS sequence is the binding site for Rph1 protein. Numbering at the top of the figure is relative to the first ATG translational start codon in the coding sequence. (Adapted from reference .)

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–12
Effect of derepression of the yeast gene on the survival of nucleotide excision repair-defective strains exposed to UV radiation. Cells that are mutant for both the and genes show increased survival. WT, wild type. (Adapted from reference .)
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Figure 4–12

Effect of derepression of the yeast gene on the survival of nucleotide excision repair-defective strains exposed to UV radiation. Cells that are mutant for both the and genes show increased survival. WT, wild type. (Adapted from reference .)

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–13
The Rph1 and Gis1 proteins have amino acid sequence identity and similarity. The region near the C terminus shows almost 100% amino acid identity and contains two zinc finger motifs. Amino acids in these motifs that are thought to be involved in binding DNA are over-lined. (Adapted from reference .)
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Figure 4–13

The Rph1 and Gis1 proteins have amino acid sequence identity and similarity. The region near the C terminus shows almost 100% amino acid identity and contains two zinc finger motifs. Amino acids in these motifs that are thought to be involved in binding DNA are over-lined. (Adapted from reference .)

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–14
Amino acid sequence comparison of DNA photolyases from (E.c.), serovar Typhimurium (S.t.), (A.n.), and Identical amino acids in all seven polypeptides are indicated in light gold, and conservative substitutions are indicated in dark gold. Asterisks represent unrelated amino acids, and the numbers in parentheses indicate amino acid distances separating conserved domains. The first 71 amino acids of the polypeptide are not shown. (Adapted from reference .)
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Figure 4–14

Amino acid sequence comparison of DNA photolyases from (E.c.), serovar Typhimurium (S.t.), (A.n.), and Identical amino acids in all seven polypeptides are indicated in light gold, and conservative substitutions are indicated in dark gold. Asterisks represent unrelated amino acids, and the numbers in parentheses indicate amino acid distances separating conserved domains. The first 71 amino acids of the polypeptide are not shown. (Adapted from reference .)

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–15
(A) Breakage (dotted gold line) of the cyclobutane ring in a thymine-thymine CPD generates two canonical thymines. (B) However, cleavage of the C-6/C-4 bond linking two thymines in a (6–4)PP would not yield normal products. (Adapted from reference .)
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Figure 4–15

(A) Breakage (dotted gold line) of the cyclobutane ring in a thymine-thymine CPD generates two canonical thymines. (B) However, cleavage of the C-6/C-4 bond linking two thymines in a (6–4)PP would not yield normal products. (Adapted from reference .)

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–16
A factor in extracts of repairs (6–4)PP in UV-irradiated plasmid DNA. UV-irradiated plasmid DNA was incubated with extract in the presence (gold line) or absence (black broken line) of fluorescent light and then treated with PDDNA photolyase to remove CPD. The plasmid DNA was then transformed into an strain defective for PD-DNA photolyase activity and nucleotide excision repair. Transforming activity was not observed when the plasmid DNA was exposed to fluorescent light in the absence of extract (solid black line). (Adapted from reference .)
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Figure 4–16

A factor in extracts of repairs (6–4)PP in UV-irradiated plasmid DNA. UV-irradiated plasmid DNA was incubated with extract in the presence (gold line) or absence (black broken line) of fluorescent light and then treated with PDDNA photolyase to remove CPD. The plasmid DNA was then transformed into an strain defective for PD-DNA photolyase activity and nucleotide excision repair. Transforming activity was not observed when the plasmid DNA was exposed to fluorescent light in the absence of extract (solid black line). (Adapted from reference .)

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–17
Amino acid sequence alignment of regions of (6–4)PP- and PD-DNA photolyases in the FAD-binding (A) and active-site (B) regions. The lighter gold boxes show conservation of amino acids, especially aromatic residues. The dark gold boxes indicate conserved histidine residues in the proposed active site of the (6–4)PP-DNA photolyases. (Adapted from reference .)
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Figure 4–17

Amino acid sequence alignment of regions of (6–4)PP- and PD-DNA photolyases in the FAD-binding (A) and active-site (B) regions. The lighter gold boxes show conservation of amino acids, especially aromatic residues. The dark gold boxes indicate conserved histidine residues in the proposed active site of the (6–4)PP-DNA photolyases. (Adapted from reference .)

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–18
Proposed mechanism for photoreactivation of (6–4)PP by (6–4)PP-DNA photolyase. The mechanism involves two histidine residues (His354 and His358) located at the active site (see Fig. 4–17 ). His354 and His358 hydrogen bond with the N-3 of the 3’ pyrimidone and with the OH-group of the 5’ pyrimidone, respectively. His358 abstracts a proton from the OH-group (or from the protonated amino group at C-5) of the 5’ pyrimidine, and His354 protonates N-3 of the 3’ pyrimidone. Nucleophilic attack at the cationic 3’ C-4 results in the formation of an oxetane intermediate. As is the case with PD-DNA photolyases, light absorbed by a photoantenna (not shown here) generates excitation energy that is transferred to the active-site flavin (FADH). Electron transfer results in the conversion of the oxetane intermediate to native thymines and transfer of an electron back to the ground-state flavin neutral radical. (Adapted from reference .)
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Figure 4–18

Proposed mechanism for photoreactivation of (6–4)PP by (6–4)PP-DNA photolyase. The mechanism involves two histidine residues (His354 and His358) located at the active site (see Fig. 4–17 ). His354 and His358 hydrogen bond with the N-3 of the 3’ pyrimidone and with the OH-group of the 5’ pyrimidone, respectively. His358 abstracts a proton from the OH-group (or from the protonated amino group at C-5) of the 5’ pyrimidine, and His354 protonates N-3 of the 3’ pyrimidone. Nucleophilic attack at the cationic 3’ C-4 results in the formation of an oxetane intermediate. As is the case with PD-DNA photolyases, light absorbed by a photoantenna (not shown here) generates excitation energy that is transferred to the active-site flavin (FADH). Electron transfer results in the conversion of the oxetane intermediate to native thymines and transfer of an electron back to the ground-state flavin neutral radical. (Adapted from reference .)

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–19
Phylogenetic relationships between blue-light receptor proteins. Shown are photolyases and CRY proteins from (Nc), (Sc), (Ec), serovar Typhimurium (St), (Hh), (Cr), (Md), (Mt), zebrafish (Z), (Hs), and (X1). PD-DNA photolyases (CPD), (6–4)PP-DNA photolyases ( ), and CRY proteins (CRY or CRT) are shown. (Adapted from reference .)
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Figure 4–19

Phylogenetic relationships between blue-light receptor proteins. Shown are photolyases and CRY proteins from (Nc), (Sc), (Ec), serovar Typhimurium (St), (Hh), (Cr), (Md), (Mt), zebrafish (Z), (Hs), and (X1). PD-DNA photolyases (CPD), (6–4)PP-DNA photolyases ( ), and CRY proteins (CRY or CRT) are shown. (Adapted from reference .)

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–20
Oligonucleotide constructs used to examine deoxyribozyme activity on CPD. A 35-nucleotide element consisting of 20- and 15-mer oligonucleotides linked through a T<>T dimer but lacking a connecting phosphodiester linkage was hybridized to a perfectly complementary 25-nucleotide splint (A), a “flipped” splint in which the two A residues complementary to the T<>T were deleted (B), and a “mismatched” splint in which AA was replaced by either TT or CC, generating mismatches with the dimer (IC). (Adapted from reference )
10.1128/9781555816704/f0132-02_thmb.gif
10.1128/9781555816704/f0132-02.gif
Image of Figure 4–20
Figure 4–20

Oligonucleotide constructs used to examine deoxyribozyme activity on CPD. A 35-nucleotide element consisting of 20- and 15-mer oligonucleotides linked through a T<>T dimer but lacking a connecting phosphodiester linkage was hybridized to a perfectly complementary 25-nucleotide splint (A), a “flipped” splint in which the two A residues complementary to the T<>T were deleted (B), and a “mismatched” splint in which AA was replaced by either TT or CC, generating mismatches with the dimer (IC). (Adapted from reference )

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–21
Structure of SP (bottom). The structure of a CPD (top) is shown for comparison. (Adapted from reference .)
10.1128/9781555816704/f0133-01_thmb.gif
10.1128/9781555816704/f0133-01.gif
Image of Figure 4–21
Figure 4–21

Structure of SP (bottom). The structure of a CPD (top) is shown for comparison. (Adapted from reference .)

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–22
A plasmid containing the gene of confers UV radiation resistance to spores of strains that are mutant for , regardless of whether they are proficient or defective (uvrA) in nucleotide excision repair. (Adapted from reference .)
10.1128/9781555816704/f0133-02_thmb.gif
10.1128/9781555816704/f0133-02.gif
Image of Figure 4–22
Figure 4–22

A plasmid containing the gene of confers UV radiation resistance to spores of strains that are mutant for , regardless of whether they are proficient or defective (uvrA) in nucleotide excision repair. (Adapted from reference .)

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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Figure 4–23
Proposed mechanism for the repair of SP. Two subunits of SplB protein dimerize through the formation of a reduced [4Fe-4S] center to form active SP lyase (not shown). The [4Fe-4S] center donates an electron(s) to SAM, generating methionine and a 5’-adenosyl radical (top). The latter moiety is used to abstract a proton from C-6’ of SP, leading to β-scission of the bond linking the thymines and completion of the reaction by back transfer of the proton (bottom). dRib, deoxyribose. (Adapted from reference .)
10.1128/9781555816704/f0134-01_thmb.gif
10.1128/9781555816704/f0134-01.gif
Image of Figure 4–23
Figure 4–23

Proposed mechanism for the repair of SP. Two subunits of SplB protein dimerize through the formation of a reduced [4Fe-4S] center to form active SP lyase (not shown). The [4Fe-4S] center donates an electron(s) to SAM, generating methionine and a 5’-adenosyl radical (top). The latter moiety is used to abstract a proton from C-6’ of SP, leading to β-scission of the bond linking the thymines and completion of the reaction by back transfer of the proton (bottom). dRib, deoxyribose. (Adapted from reference .)

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
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References

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1. Ahmad, M., and, A. R. Cashmore. 1993. HY4 gene of A. thaliana encodes a protein with characteristics of a blue-light photoreceptor. Nature 366 :162– 166.
2. Aubert, C.,, M. H. Vos,, P. Mathis,, A. P. Eker, and, K. Brettel. 2000. Intraprotein radical transfer during photoactivation of DNA photolyase. Nature 405 :586– 590.
3. Baer, M. E., and, G. B. Sancar. 1993. The role of conserved amino acids in substrate binding and discrimination by photolyase. J. Biol. Chem. 268 :16717– 16724.
4. Benbow, R. M.,, A. J. Zuccarelli, and, R. L. Sinsheimer. 1974. A role for single-strand breaks in bacteriophage phi-X174 genetic recombination. J. Mol. Biol. 88 :629– 651.
5. Bennetzen, J. L., and, B. D. Hall. 1982. Codon selection in yeast. J. Biol. Chem. 257 :3026– 3031.
6. Berg, O. G.,, R. B. Winter, and, P. H. von Hipple. 1982. How do genome-regulatory proteins locate their DNA target sites? Trends Biochem. Sci. 7 :52– 55.
7. Birrell, G. W.,, J. A. Brown,, H. I. Wu,, G. Giaever,, A. M. Chu,, R. W. Davis, and, J. M. Brown. 2002. Transcriptional response of Saccharomyces cerevisiae to DNA-damaging agents does not identify the genes that protect against these agents. Proc. Natl. Acad. Sci. USA 99 :8778– 8783.
8. Branum, M. E.,, J. T. Reardon, and, A. Sancar. 2001. DNA repair excision nuclease attacks undamaged DNA. A potential source of spontaneous mutations. J. Biol. Chem. 276 :25421– 25426.
9. Caillet-Fauquet, P.,, M. Defais, and, M. Radman. 1977. Molecular mechanisms of induced mutagenesis. Replication in vivo of bacteriophage phiX174 single-stranded, ultraviolet light-irradiated DNA in intact and irradiated host cells. J. Mol. Biol. 117 :95– 110.
10. Carell, T.,, L. T. Burgdorf,, L. M. Kundu, and, M. Cichon. 2001. The mechanism of action of DNA photolyases. Curr. Opin. Chem. Biol. 5 :491– 498.
11. Cheek, J., and, J. B. Broderick. 2002. Direct H atom abstraction from spore photoproduct C-6 initiates DNA repair in the reaction catalyzed by spore photoproduct lyase: evidence for a reversibly generated adenosyl radical intermediate. J. Am. Chem. Soc. 124 :2860– 2861.
12. Chen, J.,, C. W. Huang,, L. Hinman,, M. P. Gordon, and, D. A. Deranleau. 1976. Photomonomerization of pyrimidine dimers by indoles and proteins. J. Theor. Biol. 62 :53– 67.
13. Chinnapen, D. J., and, D. Sen., 2004. A deoxyribozyme that harnesses light to repair thymine dimers in DNA. Proc. Natl. Acad. Sci. USA 101: 65– 69.
14. Cook, J. S., 1970. Photoreactivation in animal cells. Photophysiology 5 :191– 233.
15. Dany, A. L.,, T. Douki,, C. Triantaphylides, and, J. Cadet. 2001. Repair of the main UV-induced thymine dimeric lesions within Arabidopsis thaliana DNA: evidence for the major involvement of photoreactivation pathways. J. Photochem. Photobiol. Ser. B. 65 :127– 135.
16. Deisenhofer, J., 2000. DNA photolyases and cryptochromes. Mutat. Res. 460 :143– 149.
17. Dulbecco, R., 1949. Reactivation of ultraviolet inactivated bacteriophage by visible light. Nature (London) 163 :949– 950.
18. Eker, A. P.,, R. H. Dekker, and, W. Berends. 1981. Photoreactivating enzyme from Streptomyces griseus. IV. On the nature of the chromophoric cofactor in Streptomyces griseus photoreactivating enzyme. Photochem. Photobiol. 33 :65– 72.
19. Eker, A. P., and, A. M. Fichtinger-Schepman. 1975. Studies on a DNA photoreactivating enzyme from Streptomyces griseus. II. Purification of the enzyme. Biochim. Biophys. Acta 378 :54– 63.
20. Eker, A. P.,, J. K. Hessels, and, R. H. Dekker. 1986. Photoreactivating enzyme from Streptomyces griseus. VI. Action spectrum and kinetics of photoreactivation. Photochem. Photobiol. 44 :197– 205.
21. Eker, A. P.,, P. Kooiman,, J. K. Hessels, and, A. Yasui. 1990. DNA photoreactivating enzyme from the cyanobacterium Anacystis nidulans. J. Biol. Chem. 265 :8009– 8015.
22. Eker, A. P.,, H. Yajima, and, A. Yasui., 1994. DNA photolyase from the fungus Neurospora crassa. Purification, characterization and comparison with other photolyases. Photochem. Photobiol. 60 :125– 133.
23. Eker, A. P. M.,, J. K. C. Hessels, and, J. van de Velde. 1988. Photoreactivating exzyme from the green alga Scenedesmus acutus. Evidence from the presence of two different flavin chromophores. Biochemistry 27 :1758– 1765.
24. Eker, A. P. M.,, L. Formenoy, and, L. Dewit. 1991. Photoreactivation in the extreme halophilic archaebacterium Halobacterium cutirubrum. Photochem. Photobiol. 53 :643– 651.
25. Epple, R., and, T. Carell. 1999. Efficient light-dependent DNA repair requires a large cofactor separation. J. Am. Chem. Soc. 121 :7318– 7329.
26. Epple, R., and, T. Carell. 1998. Flavin- and deazaflavin-containing model compounds mimic the energy transfer step in type II DNAphotolyases. Angew. Chem. Int. Ed. Engl. 37 :938– 941.
27. Fajardo-Cavazos, P., and, W. L. Nicholson. 1995. Molecular dissection of mutations in the Bacillus subtilis spore photoproduct lyase gene which affect repair of spore DNA damage caused by UV radiation. J. Bacteriol. 177 :4402– 4409.
28. Fajardo-Cavazos, P.,, C. Salazar, and, W. L. Nicholson. 1993. Molecular cloning and characterization of the Bacillus subtilis spore photoproduct lyase (spl) gene, which is involved in repair of UV radiation-induced DNA damage during spore germination. J. Bacteriol. 175 :1735– 1744.
29. Farland, W. H., and, B. M. Sutherland. 1981. Analysis of pyrimidine dimer content of isolated DNA by nuclease digestion, p. 45– 56. In E. C. Friedberg and P. C. Hanawalt (ed.), DNA Repair: a Laboratory Manual of Research Procedures, vol., 1, part A. Marcel Dekker, Inc., New York, N.Y.
30. Friedberg, E. C., 1997. Correcting the Blueprint of Life: a Historical Account of the Discovery of DNA Repair Mechanisms. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
31. Friedberg, E. C., and, P. C. Hanawalt. 1981. DNA Repair: a Laboratory Manual of Research Procedures, vol. 1, part A. Marcel Dekker, Inc., New York, N.Y.
32. Friedberg, E. C., and, P. C. Hanawalt. 1983. DNA Repair: a Laboratory Manual of’Research Procedures, vol. 2. Marcel Dekker, Inc., New York, N.Y.
33. Friedberg, E. C.,, G. C. Walker, and, W. Siede. 1995. DNA Repair and Mutagenesis. ASM Press, Washington, D.C.
34. Gilbert, W., 1986. The RNA world. Nature 319 :618.
35. Gordon, M. P., 1975. Photorepair of RNA. Basic Life Sci. 5A :115– 121.
36. Hahn, J.,, M. E. Michel-Beyerle, and, N. Rosch. 1999. Binding of pyrimidine model dimers to the photolyase enzyme: a molecular dynamics study. J. Phys. Chem. Ser. B 103 :2001– 2007.
37. Hanawalt, P. C., 2002. Subpathways of nucleotide excision repair and their regulation. Oncogene 21 :8949– 8956.
38. Harm, H., and, C. S. Rupert. 1970. Analysis of photoenzymatic repair of UV lesions in DNA by single light flashes. VII. Photolysis of enzyme-substrate complexes in vitro. Mutat. Res. 10 :307– 318.
39. Harm, W., 1970. Analysis of photoenzymatic repair of UV lesions in DNA by single light flashes. V. Determination of the reaction-rate constants in E. coli cells. Mutat. Res. 10 :277– 290.
40. Harm, W., 1975. Kinetics of photoreactivation. Basic Life Sci. 5A :89– 101.
41. Harm, W.,, H. Harm, and, C. S. Rupert. 1968. Analysis of photoenzymatic repair of UV lesions in DNA by single light flashes. II. In vivo studies with Escherichia coli cells and bacteriophage. Mutat. Res. 6 :371– 385.
42. Harm, W.,, C. S. Rupert, and, H. Harm. 1972. Photoenzymatic repair of DNA. I. Investigation of the reaction by flash illumination. Johns Hopkins Med. J. Suppl. 1 :53– 78.
43. Heelis, P. F.,, G. Payne, and, A. Sancar. 1987. Photochemical properties of Escherichia coli DNA photolyase: selective photodecomposition of the second chromophore. Biochemistry 26 :4634– 4640.
44. Helene, C., and, M. Charlier. 1977. Photosensitized splitting of pyrimidine dimers by indole derivatives and by tryptophan-containing oligopeptides and proteins. Photochem. Photobiol. 25 :429– 434.
45. Helene, C.,, M. Charlier,, J. J. Toulme, and, F. Toulme. 1978. Photosensitized splitting of thymine dimers in DNA by peptides and protein containing tryptophanyl residues, p. 141– 146. In P. C. Hanawalt,, E. C. Fried-berg, and, C. F. Fox (ed.), DNA Repair Mechanisms. Academic Press, Inc., New York, N.Y.
46. Hidema, J.,, T. Kumagai, and, B. M. Sutherland. 2000. UV radiation-sensitive norin 1 rice contains defective cyclobutane pyrimidine dimer photolyase. Plant Cell 12 :1569– 1578.
47. Hitomi, K.,, S. T. Kim,, S. Iwai,, N. Harima,, E. Otoshi,, M. Ikenaga, and, T. Todo. 1997. Binding and catalytic properties of Xenopus (6–4) photolyase. J. Biol. Chem. 272 :32591– 32598.
48. Hitomi, K.,, H. Nakamura,, S. T. Kim,, T. Mizukoshi,, T. Ishikawa,, S. Iwai, and, T. Todo. 2001. Role of two histidines in the (6–4) photolyase reaction. J. Biol. Chem. 276 :10103– 10109.
49. Hurter, J.,, M. P. Gordon,, J. P. Kirwan, and, A. D. McLaren. 1974. In vitro photoreactivation of ultraviolet-inactivated ribonucleic acid from tobacco mosaic virus. Photochem. Photobiol. 19 :185– 190.
50. Husain, I., and, A. Sancar. 1987. Binding of E. coli DNA photolyase to a defined substrate containing a single T mean value of T dimer. Nucleic Acids Res. 15 :1109– 1120.
51. Husain, I., and, A. Sancar. 1987. Photoreactivation in phr mutants of Escherichia coli K-12. J. Bacteriol. 169 :2367– 2372.
52. Husain, I.,, G. B. Sancar,, S. R. Holbrook, and, A. Sancar. 1987. Mechanism of damage recognition by Escherichia coli DNA photolyase. J. Biol. Chem. 262 :13188– 13197.
53. Iwatsuki, N.,, C. O. Joe, and, H. Werbin. 1980. Evidence that deoxyribonucleic acid photolyase from baker’s yeast is a flavoprotein. Biochemistry 19 :1172– 1176.
54. Jang, Y. K.,, L. Wang, and, G. B. Sancar. 1999. RPH1 and GIS1 are damage-responsive repressors of PHR1. Mol. Cell. Biol. 19 :7630– 7638.
55. Johnson, J. L.,, S. Hamm-Alvarez,, G. Payne,, G. B. Sancar,, K. V. Rajagopalan, and, A. Sancar. 1988. Identification of the second chromophore of Escherichia coli and yeast DNA photolyases as 5,10-methenyltetrahydrofolate. Proc. Natl. Acad. Sci. USA 85 :2046– 2050.
56. Jordan, S. P.,, J. L. Alderfer,, L. P. Chanderkar, and, M. S. Jorns. 1989. Reaction of Escherichia coli and yeast photolyases with homogeneous short-chain oligonucleotide substrates. Biochemistry 28 :8149– 8153.
57. Jordan, S. P., and, M. S. Jorns. 1988. Evidence for a singlet intermediate in catalysis by Escherichia coli DNA photolyase and evaluation of substrate binding determinants. Biochemistry 27 :8915– 8923.
58. Jorns, M. S.,, G. B. Sancar, and, A. Sancar. 1984. Identification of a neutral flavin radical and characterization of a second chromophore in Escherichia coli DNA photolyase. Biochemistry 23 :2673– 2679.
59. Jorns, M. S.,, G. B. Sancar, and, A. Sancar. 1985. Identification of oligothymidylates as new simple substrates for Escherichia coli DNA photolyase and their use in a rapid spectrophotometric enzyme assay. Biochemistry 24 :1856– 1861.
60. Jorns, M. S.,, B. Wang, and, S. P. Jordan. 1987. DNA repair catalyzed by Escherichia coli DNA photolyase containing only reduced flavin: elimination of the enzyme’s second chromophore by reduction with sodium borohydride. Biochemistry 26 :6810– 6816.
61. Jorns, M. S.,, B. Y. Wang,, S. P. Jordan, and, L. P. Chanderkar. 1990. Chromophore function and interaction in Escherichia coli DNA photolyase: reconstitution of the apoenzyme with pterin and/or flavin derivatives. Biochemistry 29 :552– 561.
62. Kelner, A., 1949. Effect of visible light on the recovery of Streptomyces griseus conidia from ultra-violet irradiation injury. Proc. Natl. Acad. Sci. USA 52 :73– 79.
63. Kiener, A.,, I. Husain,, A. Sancar, and, C. Walsh. 1989. Purification and properties of Methanobacterium thermoautotrophicum DNA photolyase. J. Biol. Chem. 264 :13880– 13887.
64. Kim, S. T.,, K. Malhotra,, H. Ryo,, A. Sancar, and, T. Todo. 1996. Purification and characterization of Drosophila melanogaster photolyase. Mutat. Res. 363 :97– 104.
65. Kim, S. T.,, K. Malhotra,, C. A. Smith,, J. S. Taylor, and, A. Sancar. 1994. Characterization of (6–4) photoproduct DNA photolyase. J. Biol. Chem. 269 :8535– 8540.
66. Kim, S. T., and, A. Sancar. 1991. Effect of base, pentose, and phosphodiester backbone structures on binding and repair of pyrimidine dimers by Escherichia coli DNA photolyase. Biochemistry 30 :8623– 8630.
67. Kim, S. T., and, A. Sancar. 1993. Photochemistry, photophysics, and mechanism of pyrimidine dimer repair by DNA photolyase. Photochem. Photobiol. 57 :895– 904.
68. Kim, S. T., and, A. Sancar. 1995. Photorepair of nonadjacent pyrimidine dimers by DNA photolyase. Photochem. Photobiol. 61 :171– 174.
69. Kleiner, O.,, J. Butenandt,, T. Carell, and, A. Batschauer. 1999. Class II DNA photolyase from Arabidopsis thaliana contains FAD as a cofactor. Eur. J. Biochem. 264 :161– 167.
70. Kobayashi, T.,, M. Takao,, A. Oikawa, and, A. Yasui. 1990. Increased UV sensitivity of Escherichia coli cells after introduction of foreign photolyase genes. Mutat. Res. 236 :27– 34.
71. Kobayashi, T.,, M. Takao,, A. Oikawa, and, A. Yasui. 1989. Molecular characterization of a gene encoding a photolyase from Streptomyces griseus. Nucleic Acids Res. 17 :4731– 4744.
72. Komori, H.,, R. Masui,, S. Kuramitsu,, S. Yokoyama,, T. Shibata,, Y. Inoue, and, K. Miki. 2001. Crystal structure of thermostable DNA photolyase: pyrimidine-dimer recognition mechanism. Proc. Natl. Acad. Sci. USA 98 :13560– 13565.
73. Landry, L. G.,, A. E. Stapleton,, J. Lim,, P. Hoffman,, J. B. Hays,, V. Walbot, and, R. L. Last. 1997. An Arabidopsis photolyase mutant is hypersensitive to ultraviolet-B radiation. Proc. Natl. Acad. Sci. USA 94 :328– 332.
74. Langeveld, S. A.,, A. Yasui, and, A. P. Eker. 1985. Expression of an Escherichia coli phr gene in the yeast Saccharomyces cerevisiae. Mol. Gen. Genet. 199 :396– 400.
75. Lau, A. Y.,, O. D. Scharer,, L. Samson,, G. L. Verdine, and, T. Ellenberger. 1998. Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision. Cell 95 :249– 258.
76. Li, Y. F.,, S. T. Kim, and, A. Sancar. 1993. Evidence for lack of DNA photoreactivating enzyme in humans. Proc. Natl. Acad. Sci. USA 90 :4389– 4393.
77. Li, Y. F., and, A. Sancar. 1991. Cloning, sequencing, expression and characterization of DNA photolyase from Salmonella typhimurium. Nucleic Acids Res. 19 :4885– 4890.
78. Lin, C.,, H. Yang,, H. Guo,, T. Mockler,, J. Chen, and, A. R. Cash-more. 1998. Enhancement of blue-light sensitivity of Arabidopsis seedlings by a blue light receptor cryptochrome 2. Proc. Natl. Acad. Sci. USA 95 :2686– 2690.
79. Madden, J. J., and, H. Werbin. 1974. Use of membrane binding technique to study the kinetics of yeast deoxyribonucleic acid photolyase reactions. Formation of enzyme-substrate complexes in the dark and their photolysis. Biochemistry 13 :2149– 2154.
80. Madden, J. J.,, H. Werbin, and, J. Denson. 1973. A rapid assay for DNA photolyase using a membrane-binding technique. Photochem. Photobiol. 18 :441– 445.
81. Malhotra, K.,, M. Baer,, Y. F. Li,, G. B. Sancar, and, A. Sancar. 1992. Identification of chromophore binding domains of yeast DNA photolyase. J. Biol. Chem. 267 :2909– 2914.
82. Mees, A.,, T. Klar,, P. Gnau,, U. Hennecke,, A. P. M. Eker,, T. Carell, and, L.-O. Essen. 2004. Crystal structure of a photolyase bound to a CPDlike DNA lesion after in situ repair. Science 306 :1789– 1793.
83. Mehl, R. A., and, T. P. Begley. 1999. Mechanistic studies on the repair of a novel DNA photolesion: the spore photoproduct. Org. Lett. 1 :1065– 1066.
84. Miyamoto, Y., and, A. Sancar. 1998. Vitamin B2-based blue-light photoreceptors in the retinohypothalamic tract as the photoactive pigments for setting the circadian clock in mammals. Proc. Natl. Acad. Sci. USA 95 :6097– 6102.
85. Moore, P., and, B. S. Strauss. 1979. Sites of inhibition of in vitro DNA synthesis in carcinogen- and UV-treated phi X174 DNA. Nature (London) 278 :664– 666.
86. Nicholson, W. L.,, L. Chooback, and, P. Fajardo-Cavazos. 1997. Analysis of spore photoproduct lyase operon (splAB) function using targeted deletion-insertion mutations spanning the Bacillus subtilis operons ptsHI and splAB. Mol. Gen. Genet. 255 :587– 594.
87. Okumura, T.,, A. Sancar,, P. F. Heelis,, T. P. Begley,, Y. Hirata, and, N. Mataga. 1991. Picosecond later photolysis studies on the photorepair of pyrimidine dimers by DNA photolyase., 1. Laser photolysis of photolyase-2-deoxyuridine dinucleotide photodimer complex. J. Am. Chem. Soc. 113: 3143– 3145.
88. Ozer, Z.,, J. T. Reardon,, D. S. Hsu,, K. Malhotra, and, A. Sancar. 1995. The other function of DNA photolyase: stimulation of excision repair of chemical damage to DNA. Biochemistry 34 :15886– 15889.
89. Park, H. W.,, S. T. Kim,, A. Sancar, and, J. Deisenhofer. 1995. Crystal structure of DNA photolyase from Escherichia coli. Science 268 :1866– 1872.
90. Patrick, M., and, R. Rahn. 1976. Photochemistry of DNA and polynucleotides: photoproducts, p., 35– 95. In S. Y. Yang (ed.), Photochemistry and Photobiology of the Nucleic Acids. Academic Press, Inc., New York, N.Y.
91. Payne, G., P. F. Heelis,, B. R. Rohrs, and, A. Sancar., 1987. The active form of Escherichia coli DNA photolyase contains a fully reduced flavin and not a flavin radical, both in vivo and in vitro. Biochemistry 26 :7121– 7127.
92. Payne, G., and, A. Sancar. 1990. Absolute action spectrum of E-FADH2 and E-FADH2-MTHF forms of Escherichia coli DNA photolyase. Biochemistry 29 :7715– 7727.
93. Payne, G.,, M. Wills,, C. Walsh, and, A. Sancar. 1990. Reconstitution of Escherichia coli photolyase with flavins and flavin analogues. Biochemistry 29 :5706– 5711.
94. Petersen, J. L., and, G. D. Small. 2001. A gene required for the novel activation of a class II DNA photolyase in Chlamydomonas. Nucleic Acids Res. 29 :4472– 4481.
95. Rebeil, R., and, W. L. Nicholson. 2001. The subunit structure and catalytic mechanism of the Bacillus subtilis DNA repair enzyme spore photoproduct lyase. Proc. Natl. Acad. Sci. USA 98 :9038– 9043.
96. Rebeil, R.,, Y. Sun,, L. Chooback,, M. Pedraza-Reyes,, C. Kins-land,, T. P. Begley, and, W. L. Nicholson. 1998. Spore photoproduct lyase from Bacillus subtilis spores is a novel iron-sulfur DNA repair enzyme which shares features with proteins such as class III anaerobic ribonucleotide reductases and pyruvate-formate lyases. J. Bacteriol. 180 :4879– 4885.
97. Resnick, M. A., 1969. A photoreactivationless mutant of Saccharomyces cerevisiae. Photochem. Photobiol. 9 :307– 312.
98. Resnick, M. A., and, J. K. Setlow. 1972. Photoreactivation and gene dosage in yeast. J. Bacteriol. 109 :1307– 1309.
99. Roberts, R. J., and, X. Cheng. 1998. Base flipping. Annu. Rev. Biochem. 67 :181– 198.
100. Rupert, C. S., 1975. Enzymatic photoreactivation: overview. Basic Life Sci. 5A :73– 87.
101. Rupert, C. S., 1962. Photoenzymatic repair of ultraviolet damage in DNA. I. Kinetics of the reaction. J. Gen. Physiol. 45 :703– 724.
102. Rupert, C. S., 1962. Photoenzymatic repair of ultraviolet damage in DNA. II. Formation of an enzyme-substrate complex. J. Gen. Physiol. 45: 725– 741.
103. Rupert, C. S., 1960. Photoreactivation of transforming DNA by an enzyme from baker’s yeast. J. Gen. Physiol. 43 :573– 595.
104. Rupert, C. S., and, A. Sancar., 1978. Cloning the phr gene of Escherichia coli, p., 159– 162. In P. C. Hanawalt,, E. C. Friedberg, and, C. F. Fox (ed.), Molecular and Cellular Repair Processes. Johns Hopkins University Press, Baltimore, Md.
105. Rupert, C. S., and, W. Harm. 1966. Reactivation after photobiological damage. Adv. Radiat. Biol. 2 :1– 81.
106. Rupert, C. S.,, W. Harm, and, H. Harm. 1972. Photoenzymatic repair of DNA. II. Physical-chemical characterization of the process. Johns Hopkins Med. J. Suppl. 1 :64– 78.
107. Rupert, C. S.,, S. Goodgal, and, R. M. Herriott. 1958. Photoreactivation in vitro of ultraviolet inactivated Haemophilus influenzae transforming factor. J. Gen. Physiol. 41 :451– 471.
108. Sancar, A., 1996. No “End of History” for photolyases. Science 272 :48– 49.
109. Sancar, A., 1994. Structure and function of DNA photolyase. Biochemistry 33 :2– 9.
110. Sancar, A., 2003. Structure and function of DNA photolyase and cryptochrome blue-light photoreceptors. Chem. Rev. 103 :2203– 2237.
111. Sancar, A., and, C. S. Rupert. 1983. The phr gene of Escherichia coli, p., 241– 252. In E. C. Friedberg and, P. C. Hanawalt (ed.), DNA Repair: a Laboratory Manual of Research Procedures, vol., 2. Marcel Dekker, Inc., New York, N.Y.
112. Sancar, A.,, K. A. Franklin, and, G. B. Sancar. 1984. Escherichia coli DNA photolyase stimulates uvrABC excision nuclease in vitro. Proc. Natl. Acad. Sci. USA 81 :7397– 7401.
113. Sancar, A., and, C. S. Rupert. 1978. Cloning of the phr gene and amplification of photolyase in Escherichia coli. Gene 4 :295– 308.
114. Sancar, A., and, G. B. Sancar. 1984. Escherichia coli DNA photolyase is a flavoprotein. J. Mol. Biol. 172 :223– 227.
115. Sancar, A.,, F. W. Smith, and, G. B. Sancar. 1984. Purification of Escherichia coli DNA photolyase. J. Biol. Chem. 259 :6028– 6032.
116. Sancar, G. B., 1990. DNA photolyases: physical properties, action mechanism, and roles in dark repair. Mutat. Res. 236 :147– 160.
117. Sancar, G. B., 2000. Enzymatic photoreactivation: 50 years and counting. Mutat. Res. 451 :25– 37.
118. Sancar, G. B., 1985. Expression of a Saccharomyces cerevisiae photolyase gene in Escherichia coli. J. Bacteriol. 161 :769– 771.
119. Sancar, G. B., 1985. Sequence of the Saccharomyces cerevisiae PHR1 gene and homology of the PHR1 photolyase to E. coli photolyase. Nucleic Acids Res. 13 :8231– 8246.
120. Sancar, G. B., and, A. Sancar. 1987. Structure and function of DNA photolyases. Trends Biochem. 12 :259– 261.
121. Sancar, G. B.,, R. Ferris,, F. W. Smith, and, B. Vandeberg. 1995. Promoter elements of the PHR1 gene of Saccharomyces cerevisiae and their roles in the response to DNA damage. Nucleic Acids Res. 23 :4320– 4328.
122. Sancar, G. B.,, M. S. Jorns,, G. Payne,, D. J. Fluke,, C. S. Rupert, and, A. Sancar. 1987. Action mechanism of Escherichia coli DNA photolyase. III. Photolysis of the enzyme-substrate complex and the absolute action spectrum. J. Biol. Chem. 262 :492– 498.
123. Sancar, G. B., and, F. W. Smith. 1988. Construction of plasmids which lead to overproduction of yeast PHR1 photolyase in Saccharomyces cerevisiae and Escherichia coli. Gene 64 :87– 96.
124. Sancar, G. B., and, F. W. Smith. 1989. Interactions between yeast photolyase and nucleotide excision repair proteins in Saccharomyces cerevisiae and Escherichia coli. Mol. Cell. Biol. 9 :4767– 4776.
125. Sancar, G. B.,, F. W. Smith, and, P. F. Heelis. 1987. Purification of the yeast PHR1 photolyase from an Escherichia coli overproducing strain and characterization of the intrinsic chromophores of the enzyme. J. Biol. Chem. 262 :15457– 15465.
126. Sancar, G. B.,, F. W. Smith,, M. C. Lorence,, C. S. Rupert, and, A. Sancar. 1984. Sequences of the Escherichia coli photolyase gene and protein. J. Biol. Chem. 259 :6033– 6038.
127. Sancar, G. B.,, F. W. Smith,, R. Reid,, G. Payne,, M. Levy, and, A. Sancar. 1987. Action mechanism of Escherichia coli DNA photolyase. I. Formation of the enzyme-substrate complex. J. Biol. Chem. 262 :478– 485.
128. Sancar, G. B.,, F. W. Smith, and, A. Sancar. 1985. Binding of Escherichia coli DNA photolyase to UV-irradiated DNA. Biochemistry 24 :1849– 1855.
129. Sancar, G. B.,, F. W. Smith, and, A. Sancar. 1983. Identification and amplification of the E. coli phr gene product. Nucleic Acids Res. 11 :6667– 6678.
130. Sanders, D. B., and, O. Weist. 1999. A model for the enzyme-substrate complex of DNA photolyase and photodamaged DNA. J. Am. Chem. Soc. 121 :5127– 5134.
131. Schild, D.,, J. Johnston,, C. Chang, and, R. K. Mortimer. 1984. Cloning and mapping of Saccharomyces cerevisiae photoreactivation gene PHR1. Mol. Cell. Biol. 4 :1864– 1870.
132. Schul, W.,, J. Jans,, Y. M. Rijksen,, K. H. Klemann,, A. P. Eker,, J. de Wit,, O. Nikaido,, S. Nakajima,, A. Yasui,, J. H. Hoeijmakers, and, G. T. van der Horst. 2002. Enhanced repair of cyclobutane pyrimidine dimers and improved UV resistance in photolyase transgenic mice. EMBO J. 21: 4719– 4729.
133. Sebastian, J.,, B. Kraus, and, G. B. Sancar. 1990. Expression of the yeast PHR1 gene is induced by DNA-damaging agents. Mol. Cell. Biol. 10: 4630– 4637.
134. Sebastian, J., and, G. B. Sancar. 1991. A damage-responsive DNA binding protein regulates transcription of the yeast DNA repair gene PHR1. Proc. Natl. Acad. Sci. USA 88 :11251– 11255.
135. Setlow, P., 1992. I will survive: protecting and repairing spore DNA. J. Bacteriol. 174 :2737– 2741.
136. Setlow, R. B., 1968. The photochemistry, photobiology, and repair of polynucleotides. Prog. Nucleic Acid Res. Mol. Biol. 8 :257– 295.
137. Setlow, R. B.,, P. A. Swenson, and, W. L. Carrier. 1963. Thymine dimers and inhibition of DNA synthesis by ultraviolet irradiation of cells. Science 142 :1464– 1466.
138. Singh, K. K., and, L. Samson. 1995. Replication protein A binds to regulatory elements in yeast DNA repair and DNA metabolism genes. Proc. Natl. Acad. Sci. USA 92 :4907– 4911.
139. Slieman, T. A.,, R. Rebeil, and, W. L. Nicholson. 2000. Spore photoproduct (SP) lyase from Bacillus subtilis specifically binds to and cleaves SP (5-thyminyl-5,6-dihydrothymine) but not cyclobutane pyrimidine dimers in UV-irradiated DNA. J. Bacteriol. 182 :6412– 6417.
140. Sofia, H. J.,, G. Chen,, B. G. Hetzler,, J. F. Reyes-Spindola, and, N. E. Miller. 2001. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Nucleic Acids Res. 29 :1097– 1106.
141. Srinivasan, V.,, W. M. Schnitzlein, and, D. N. Tripathy. 2001. Fowlpox virus encodes a novel DNA repair enzyme, CPD-photolyase, that restores infectivity of UV light-damaged virus. J. Virol. 75 :1681– 1688.
142. Stege, H.,, L. Roza,, A. A. Vink,, M. Grewe,, T. Ruzicka,, S. GretherBeck, and, J. Krutmann. 2000. Enzyme plus light therapy to repair DNA damage in ultraviolet-B-irradiated human skin. Proc. Natl. Acad. Sci. USA 97 :1790– 1795.
143. Strich, R.,, R. T. Surosky,, C. Steber,, E. Dubois,, F. Messenguy, and, R. E. Esposito. 1994. UME6 is a key regulator of nitrogen repression and meiotic development. Genes Dev. 8 :796– 810.
144. Sutherland, B. M., 1978. Enzymatic photoreactivation of DNA, p., 113– 122. In P. C. Hanawalt,, E. C. Friedberg, and, C. F. Fox (ed.), DNA Repair Mechanisms. Academic Press, Inc., New York, N.Y.
145. Sutherland, B. M., 1975. The human leukocyte photoreactivating enzyme. Basic Life Sci. 5A :107– 113.
146. Sutherland, B. M., 1974. Photoreactivating enzyme from human leukocytes. Nature. 248 :109– 112.
147. Sutherland, B. M., 1977. Symposium on molecular mechanisms in photoreactivation. Introduction: fundamentals of photoreactivation. Photochem. Photobiol. 25 :413– 414.
148. Sutherland, B. M., and, M. J. Chamberlin. 1973. A rapid and sensitive assay for pyrimidine dimers in DNA. Anal. Biochem. 53 :168– 176.
149. Sutherland, B. M., and, R. Oliver. 1976. Culture conditions affect photoreactivating enzyme levels in human fibroblasts. Biochim. Biophys. Acta 442 :358– 367.
150. Sutherland, B. M.,, R. Oliver,, C. O. Fuselier, and, J. C. Sutherland. 1976. Photoreactivation of pyrimidine dimers in the DNA of normal and xeroderma pigmentosum cells. Biochemistry 15 :402– 406.
151. Sutherland, B. M.,, P. Runge, and, J. C. Sutherland. 1974. DNA photoreactivating enzyme from placental mammals. Origin and characteristics. Biochemistry 13 :4710– 4715.
152. Sutherland, J. C., and, K. P. Griffin. 1980. Monomerization of pyrimidine dimers in DNA by tryptophan-containing peptides: wavelength dependence. Radiat. Res. 83 :529– 536.
153. Sweet, D. H.,, Y. K. Jang, and, G. B. Sancar. 1997. Role of UME6 in transcriptional regulation of a DNA repair gene in Saccharomyces cerevisiae. Mol. Cell. Biol. 17 :6223– 6235.
154. Swenson, P. A., and, R. B. Setlow. 1966. Effects of ultraviolet radiation on macromolecular synthesis in Escherichia coli. J. Mol. Biol. 15 :201– 219.
155. Tainer, J. A., and, E. C. Friedberg. 2000. Biological implications from structures of DNA repair proteins. DNA Repair 460 :139– 141.
156. Takao, M.,, T. Kobayashi,, A. Oikawa, and, A. Yasui. 1989. Tandem arrangement of photolyase and superoxide dismutase genes in Halobacterium halobium. J. Bacteriol. 171 :6323– 6329.
157. Takao, M.,, A. Oikawa,, A. P. Eker, and, A. Yasui. 1989. Expression of an Anacystis nidulans photolyase gene in Escherichia coli: functional complementation and modified action spectrum of photoreactivation. Photochem. Photobiol. 50 :633– 637.
158. Tamada, T.,, K. Kitadokoro,, Y. Higuchi,, K. Inaka,, A. Yasui,, P. E. de Ruiter,, A. P. Eker, and, K. Miki. 1997. Crystal structure of DNA photolyase from Anacystis nidulans. Nat. Struct. Biol. 4 :887– 891.
159. Thompson, C. L., and, A. Sancar. 2002. Photolyase/cryptochrome blue-light photoreceptors use photon energy to repair DNA and reset the circadian clock. Oncogene 21 :9043– 9056.
160. Thresher, R. J.,, M. H. Vitaterna,, Y. Miyamoto,, A. Kazantsev,, D. S. Hsu,, C. Petit,, C. P. Selby,, L. Dawut,, O. Smithies,, J. S. Takahashi, and, A. Sancar. 1998. Role of mouse cryptochrome blue-light photoreceptor in circadian photoresponses. Science 282 :1490– 1494.
161. Todo, T., 1999. Functional diversity of the DNA photolyase/blue light receptor family. Mutat. Res. 434 :89– 97.
162. Todo, T.,, H. Ryo,, A. Borden,, C. Lawrence,, K. Sakaguchi,, H. Hirata, and, T. Nomura. 1997. Non-mutagenic repair of (6–4)photoproducts by (6–4)photolyase purified from Drosophila melanogaster. Mutat. Res. 385 :83– 93.
163. Todo, T.,, H. Ryo,, K. Yamamoto,, H. Toh,, T. Inui,, H. Ayaki,, T. Nomura, and, M. Ikenaga. 1996. Similarity among the Drosophila (6–4)pho-tolyase, a human photolyase homolog, and the DNA photolyase-bluelight photoreceptor family. Science 272 :109– 112.
164. Todo, T.,, H. Takemori,, H. Ryo,, M. Ihara,, T. Matsunaga,, O. Nikaido,, K. Sato, and, T. Nomura. 1993. A new photoreactivating enzyme that specifically repairs ultraviolet light-induced (6–4)photoproducts. Nature 361 :371– 374.
165. Toulme, J. J., and, C. Helene. 1977. Specific recognition of single-stranded nucleic acids. Interaction of tryptophan-containing peptides with native, denatured, and ultraviolet-irradiated DNA. J. Biol. Chem. 252: 244– 249.
166. Towill, L.,, C. W. Huang, and, M. P. Gordon. 1977. Photoreactivation of DNA-containing cauliflower mosaic virus and tobacco mosaic virus RNA on Datura. Photochem. Photobiol. 25 :249– 257.
167. Vande Berg, B. J., and, G. B. Sancar. 1998. Evidence for dinucleotide flipping by DNA photolyase. J. Biol. Chem. 273 :20276– 20284.
168. van der Horst, G. T.,, M. Muijtjens,, K. Kobayashi,, R. Takano,, S. Kanno,, M. Takao,, J. de Wit,, A. Verkerk,, A. P. Eker,, D. van Leenen,, R. Buijs,, D. Bootsma,, J. H. Hoeijmakers, and, A. Yasui. 1999. Mammalian Cry1 and Cry2 are essential for maintenance of circadian rhythms. Nature 398 :627– 630.
169. van der Spek, P. J.,, K. Kobayashi,, D. Bootsma,, M. Takao,, A. P. Eker, and, A. Yasui. 1996. Cloning, tissue expression, and mapping of a human photolyase homolog with similarity to plant blue-light receptors. Genomics 37 :177– 182.
170. van Noort, J.,, F. Orsini,, A. Eker,, C. Wyman,, B. de Grooth, and, J. Greve. 1999. DNA bending by photolyase in specific and non-specific complexes studied by atomic force microscopy. Nucleic Acids Res. 27 :3875– 3880.
171. Van Wang, T. C., and, C. S. Rupert. 1977. Evidence for the monomerization of spore photoproduct to two thymines by the light-independent “spore repair” process in Bacillus subtilis. Photochem. Photobiol. 25 :123– 127.
172. Vassylyev, D. G.,, T. Kashiwagi,, Y. Mikami,, M. Ariyoshi,, S. Iwai,, E. Ohtsuka, and, K. Morikawa. 1995. Atomic model of a pyrimidine dimer excision repair enzyme complexed with a DNA substrate: structural basis for damaged DNA recognition. Cell 83 :773– 782.
173. Villani, G.,, S. Boiteux, and, M. Radman. 1978. Mechanism of ultraviolet-induced mutagenesis: extent and fidelity of in vitro DNA synthesis on irradiated templates. Proc. Natl. Acad. Sci. USA 75 :3037– 3041.
174. Wagner, E. K.,, M. Rice, and, B. M. Sutherland. 1975. Photoreactivation of herpes simplex virus in human fibroblasts. Nature 254 :627– 628.
175. Wang, B. Y.,, S. P. Jordan, and, M. S. Jorns. 1988. Identification of a pterin derivative in Escherichia coli DNA photolyase. Biochemistry 27 :4222– 4226.
176. Waterworth, W. M.,, Q. Jiang,, C. E. West,, M. Nikaido, and, C. M. Bray. 2002. Characterization of Arabidopsis photolyase enzymes and analysis of their role in protection from ultraviolet-B radiation. J. Exp. Bot. 53 :1005– 1015.
177. Xiao, W.,, K. K. Singh,, B. Chen, and, L. Samson. 1993. A common element involved in transcriptional regulation of two DNA alkylation repair genes (MAG and MGT1) of Saccharomyces cerevisiae. Mol. Cell. Biol. 13 :7213– 7221.
178. Yasuhira, S., and, A. Yasui. 1992. Visible light-inducible photolyase gene from the goldfish Carassius auratus. J. Biol. Chem. 267 :25644– 25647.
179. Yasui, A., and, M. R. Chevallier. 1983. Cloning of photoreactivation repair gene and excision repair gene of the yeast Saccaromyces cerevisiae. Curr. Genet. 7 :191– 194.
180. Yasui, A.,, A. P. Eker, and, M. Koken. 1989. Existence and expression of photoreactivation repair genes in various yeast species. Mutat. Res. 217 :3– 10.
181. Yasui, A.,, A. P. Eker,, S. Yasuhira,, H. Yajima,, T. Kobayashi,, M. Takao, and, A. Oikawa. 1994. A new class of DNA photolyases present in various organisms including aplacental mammals. EMBO J. 13 :6143– 6151.
182. Yasui, A., and, S. A. Langeveld. 1985. Homology between the photoreactivation genes of Saccharomyces cerevisiae and Escherichia coli. Gene 36 :349– 355.
183. Yasui, A., and, W. Laskowski. 1975. Determination of the number of photoreactivating enzyme molecules per haploid Saccharomyces cells. Int. J. Radiat. Biol. Relat. Stud. Phys. Chem. Med. 28 :511– 518.
184. Zhao, X.,, J. Liu,, D. S. Hsu,, S. Zhao,, J. S. Taylor, and, A. Sancar. 1997. Reaction mechanism of (6–4) photolyase. J. Biol. Chem. 272 :32580– 32590.
185. Zhao, X., and, D. Mu. 1998. (6–4) photolyase: light-dependent repair of DNA damage. Histol. Histopathol. 13 :1179– 1182.

Tables

Reversal of Base Damage Caused by UV Radiation
Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
/content/10.1128/9781555816704.ch04.ch04tab01
Table 4–1
Kinetic and equilibrium constants for substrate binding and photolysis by DNA photolyase
Generic image for table
Table 4–1

Kinetic and equilibrium constants for substrate binding and photolysis by DNA photolyase

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
/content/10.1128/9781555816704.ch04.ch04tab02
Table 4–2
Physical, spectroscopic, and photochemical properties of DNA photolyases
Generic image for table
Table 4–2

Physical, spectroscopic, and photochemical properties of DNA photolyases

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
/content/10.1128/9781555816704.ch04.ch04tab03
Table 4–3
Properties of multiple DNA photolyases
Generic image for table
Table 4–3

Properties of multiple DNA photolyases

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
/content/10.1128/9781555816704.ch04.ch04tab04
Table 4–4
Conservation of selected residues in photolyases
Generic image for table
Table 4–4

Conservation of selected residues in photolyases

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4
/content/10.1128/9781555816704.ch04.ch04tab05
Table 4–5
Photolyase and cryptochrome in different kingdoms
Generic image for table
Table 4–5

Photolyase and cryptochrome in different kingdoms

Citation: Errol C, Graham C, Wolfram S, Richard D, Roger A, Tom E. 2006. Reversal of Base Damage Caused by UV Radiation, p 109-138. In DNA Repair and Mutagenesis, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816704.ch4

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