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Chapter 22 : Recombination Machinery: Holliday Junction-Resolving Enzymes

Author: Malcolm F. White1
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Affiliations: 1: Centre for Biomolecular Sciences, University of St. Andrews, North Haugh, St. Andrews, Fife KY16 9ST, United Kingdom
Content Type: Monograph
Publication Year: 2005

Category: Microbial Genetics and Molecular Biology; Bacterial Pathogenesis

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Recombination Machinery: Holliday Junction-Resolving Enzymes, Page 1 of 2

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Abstract:

Holliday junctions are resolved into recombinant duplex DNA species by a class of structure-specific endonucleases known as the Holliday junction-resolving enzymes. The primary cellular resolving enzyme in bacteria is RuvC, which is the main focus of this chapter. The author also talks about the RusA protein, which may act as an alternative to RuvC in some bacterial species, and attempts to place RuvC in a wider context based on our knowledge of other junction-resolving enzymes. The first cellular Holliday junction-resolving enzyme identified was RuvC from . Homologous recombination is ubiquitous among cellular life forms and many prokaryotic and eukaryotic viruses, and wherever Holliday junctions are formed, junction-resolving enzymes can be confidently expected. Resolving enzymes recognize the branched structure of the Holliday junction and introduce paired phosphodiester bond cleavages in opposing strands to collapse the junction, releasing nicked duplex DNA products. The study of homologous recombination and the Holliday junction was for many years the realm of geneticists. Holliday junction migration work has largely been driven by studies of the RuvABC resolvasome, emphasizing the continuing utility of bacteria as a model system to study some of the most interesting problems in biology.

Citation: White M. 2005. Recombination Machinery: Holliday Junction-Resolving Enzymes, p 405-412. In Higgins N (ed), The Bacterial Chromosome. ASM Press, Washington, DC. doi: 10.1128/9781555817640.ch22

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Recombination Machinery: Holliday Junction-Resolving Enzymes
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Citation: White M. 2005. Recombination Machinery: Holliday Junction-Resolving Enzymes, p 405-412. In Higgins N (ed), The Bacterial Chromosome. ASM Press, Washington, DC. doi: 10.1128/9781555817640.ch22
/content/10.1128/9781555817640.chap22.fig22-1
Figure 1

Sequence alignment of a diverse selection of RuvC homologues: ECOLI (, Swiss-Prot database accession number P24239), YERPE (, Q8ZEU7), VIBCH (, Q9KR00), NEIMA (, Q9JTU3), TREPA (, O83530), RHILO (, Q98F72), THEMA (, Q9WZ45), DEIRA (, Q9RX75), STRCO (, Q9L289), ANASP ( sp., O52751), HELPY (, O25544), CAMJE (, Q9PLU8), MYCLE (, P40834), and SYNY3 ( sp., Q55506).

10.1128/9781555817640/fig22-1_thmb.gif
10.1128/9781555817640/fig22-1.gif
Image of Figure 1
Figure 1

Sequence alignment of a diverse selection of RuvC homologues: ECOLI (, Swiss-Prot database accession number P24239), YERPE (, Q8ZEU7), VIBCH (, Q9KR00), NEIMA (, Q9JTU3), TREPA (, O83530), RHILO (, Q98F72), THEMA (, Q9WZ45), DEIRA (, Q9RX75), STRCO (, Q9L289), ANASP ( sp., O52751), HELPY (, O25544), CAMJE (, Q9PLU8), MYCLE (, P40834), and SYNY3 ( sp., Q55506).

Citation: White M. 2005. Recombination Machinery: Holliday Junction-Resolving Enzymes, p 405-412. In Higgins N (ed), The Bacterial Chromosome. ASM Press, Washington, DC. doi: 10.1128/9781555817640.ch22
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Figure 2

Sequence alignment of a selection of cellular and viral RusA homologues: AQUAE (, Swiss-Prot database accession number O67766), LEGPN (, Q9AKY6), BACSU (, Q8X556), ECOLI (, P40116), CP9330 (phage CP-933O from O157:H7, AAL89445), CP933X (phage CP-933X from O157:H7, Q8X707), and BP82 (phage BP-82, Q37873).

10.1128/9781555817640/fig22-2_thmb.gif
10.1128/9781555817640/fig22-2.gif
Image of Figure 2
Figure 2

Sequence alignment of a selection of cellular and viral RusA homologues: AQUAE (, Swiss-Prot database accession number O67766), LEGPN (, Q9AKY6), BACSU (, Q8X556), ECOLI (, P40116), CP9330 (phage CP-933O from O157:H7, AAL89445), CP933X (phage CP-933X from O157:H7, Q8X707), and BP82 (phage BP-82, Q37873).

Citation: White M. 2005. Recombination Machinery: Holliday Junction-Resolving Enzymes, p 405-412. In Higgins N (ed), The Bacterial Chromosome. ASM Press, Washington, DC. doi: 10.1128/9781555817640.ch22
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