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Chapter 1 : Two-Component Systems

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Two-Component Systems, Page 1 of 2

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Abstract:

Among the many regulatory schemes governing virulence potential, two-component systems have been found time and time again to play key roles. The structure-function relationships of the various domains, kinase, receiver, and HPt domains, of two-component systems are examined in this chapter, following the path of information from outside to inside a bacterial cell. For each domain the general state of knowledge are presented as it relates to two-component systems in general, and then illustrated, when appropriate, with examples from the BvgAS system governing expression of toxins and other virulence factors in . Two-component systems are found regulating not only the structural genes for toxins and other virulence genes but also other regulators. As more of previously dependable antibiotic therapies are becoming less effective against bacterial infections, other modalities for the control of infectious disease are being investigated. Two approaches to this problem are the development of new vaccines and the discovery or creation of new anti-infective compounds. One approach to vaccine development involves the attenuation of organisms to create a live vaccine strain that can colonize and engender a strong and effective immune response without causing a harmful infection. Historically, this has been accomplished simply by growth of the bacterium in vitro for many generations to allow it to lose virulence characteristics. Several features of two-component systems suggest the new anti-infective compounds as potential targets for hopeful drug designers.

Citation: Stibitz S. 2003. Two-Component Systems, p 3-24. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch1

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Figures

Image of Figure 1
Figure 1

Two commonly encountered organizational schemes of two-component signaling modules. (A) The “paradigmatic” two-component system that undergoes phosphotransfer from the sensor kinase protein to the response regulator protein is pictured. (B) A “hybrid” or “unorthodox” sensor kinase, which participates in a phosphorelay mechanism, involves two additional modules but ultimately leads to the same result, phosphorylation of the receiver domain of the response regulator. Symbols: TM, transmembrane region; H, catalytic histidine; D, catalytic aspartic acid; P, phosphate. The path of phosphate transfer is shown by curved arrows. Rectangles represent conserved domains, and ellipses represent divergent domains. The extents of different domains that are discussed in the text are delineated below each example. The vertical gray bar represents the inner membrane of gram-negative organisms or the cytoplasmic membrane of gram-positive organisms. Nomenclature for the proteins and modules of two-component systems continues to evolve. The nomenclature presented here is used throughout this chapter.

Citation: Stibitz S. 2003. Two-Component Systems, p 3-24. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch1
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Image of Figure 2
Figure 2

Highly conserved residues among the conserved domains of twocomponent systems. For the histidine kinase, these residues are represented by the H, N, G1, F, and G2 boxes indicated, with consensus sequences shown. For the receiver domain, important residues are shown, numbered as for the CheY protein of The actual residue numbers of different receiver domains vary slightly, although the overall linear relationship is highly conserved. For positions where at least 70% of the sequences show the same residue, letters indicate that residue. For positions where 50% of aligned sequences have an amino acid of the same chemical family, symbols indicate that family. Positions with less than 50% conservation are indicated by black dots. Symbols: open circles, nonpolar (I, L, M, V); filled circles, polar (A, G, P, S, T); circles with plus signs, basic (H, K, R); circles with minus signs, acidic or amidic (D, E, N, Q). Residues directly participating in phosphotransfer are starred. Adapted from reference 6 with permission.

Citation: Stibitz S. 2003. Two-Component Systems, p 3-24. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch1
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Image of Figure 3
Figure 3

NMR solution structure of the dimeric core domain of EnvZ. The protein structure is depicted in ribbon format showing the four-helix bundle formed from two identical monomers. The catalytic histidine at position 243 is shown in ball-and-stick format. Based on structural coordinates deposited in the Research Collaboratory for Structural Bioinformatics (RCSB) Protein Data Bank (PDB), as described in reference 10. (See Color Plates following p. 256.)

Citation: Stibitz S. 2003. Two-Component Systems, p 3-24. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch1
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Image of Figure 4
Figure 4

NMR solution structure of the catalytic kinase domain of EnvZ. The protein structure is depicted in ribbon format. The segments corresponding to the conserved N, G1, F, and G2 boxes are colored blue, and key residues from these are shown in ball-and-stick format. This structure was determined in the presence of the nonhydrolyzable ATP analog AMP-PNP, which is shown in green ball-and-stick format. Based on structural coordinates deposited in the RCSB PDB, as described in reference 8. (See Color Plates p. 256.)

Citation: Stibitz S. 2003. Two-Component Systems, p 3-24. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch1
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Image of Figure 5
Figure 5

CheY structure determined by X-ray crystallography. The structure of CheY is presented as representative of the common structure of receiver domains from many sources. The protein structure is shown in ribbon format, and the α-helical and -strand segments are numbered. Key residues introduced in Fig. 2 are shown in blue ball-and-stick format. Two views are shown for clarity. Based on structural coordinates deposited in the RCSB PDB, as described in reference 7. (See Color Plates following p. 256.)

Citation: Stibitz S. 2003. Two-Component Systems, p 3-24. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch1
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Image of Figure 6
Figure 6

Structure of the monomeric HPt domain from the ArcB sensor kinase of determined by X-ray crystallography. Protein structure is shown in ribbon format, with the catalytic histidine at position 717 shown in blue ball-and-stick format. Based on structural coordinates deposited in the RCSB PDB, as described in reference 3. (See Color Plates following p. 256.)

Citation: Stibitz S. 2003. Two-Component Systems, p 3-24. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch1
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Image of Figure 7
Figure 7

Structure of Spo0B (A) and a complex between Spo0F and Spo0B (B) determined by X-ray crystallography. (A) The structure of a Spo0B dimer is presented as representative of the overall structure of histidine kinase domains. Protein structure is shown in ribbon format while catalytic histidines are shown in blue ball-and-stick format. Based on structural coordinates deposited in the RCSB PDB, as described in reference 11. (B) The structure of a complex between a Spo0B dimer and two cognate receiver domains of Spo0F. Based on structural coordinates deposited in the RCSB PDB, as described in reference 13. (See Color Plates p. 256.)

Citation: Stibitz S. 2003. Two-Component Systems, p 3-24. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch1
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References

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1. Chang, C.-H.,, and S. C. Winans. 1992. Functional roles assigned to the periplasmic, linker, and receiver domains of the Agrobacterium tumefaciens VirA protein. J. Bacteriol. 174:70337039.
2. Deora, R.,, H. J. Bootsma,, J. F. Miller,, and P. A. Cotter. 2001. Diversity in the Bordetella virulence regulon: transcriptional control of a Bvg-intermediate phase gene. Mol. Microbiol. 40:669683.
3. Kato, M.,, T. Mizuno,, T. Shimizu,, and T. Hakoshima. 1997. Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB. Cell 88:717723.
4. Kern, D.,, B. F. Volkman,, P. Luginbühl,, M. J. Nohalle,, S. Kustu,, and D. E. Wemmer. 1999. Structure of a transiently phosphorylated switch in bacterial signal transduction. Nature 402:894898.
5. Merkel, T. J.,, S. Stibitz,, J. M. Keith,, M. Leef,, and R. Shahin. 1998. Contribution of regulation by the bvg locus to respiratory infection of mice by Bordetella pertussis. Infect. Immun. 66:43674373.
6. Parkinson, J. S.,, and E. C. Kofoid. 1992. Communication modules in bacterial signaling proteins. Annu. Rev. Genet. 26:71112.
7. Stock, A. M.,, E. Martinez-Hackert,, B. F. Rasmussen,, A. H. West,, J. B. Stock,, D. Ringe,, and G. A. Petsk. 1993. Structure of the Mg2+-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis. Biochemistry 32:1337513380.
8. Tanaka, T.,, S. K. Saha,, C. Tomomori,, R. Ishima,, D. Liu,, K. I. Tong,, H. Park,, R. Dutta,, L. Qin,, M. B. Swindells,, T. Yamazaki,, A. M. Ono,, M. Kainosho,, M. Inouye,, and M. Ikura. 1998. NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ. Nature 396:8892.
9. Taylor, B. L.,, and I. B. Zhulin. 1999. PAS domains: internal sensors of oxygen, redox potential, and light. Microbiol. Mol. Biol. Rev. 63:479506.
10. Tomomori, C.,, T. Tanaka,, R. Dutta,, H. Park,, S. K. Saha,, Y. Zhu,, R. Ishima,, D. Liu,, K. I. Tong,, H. Kurokawa,, H. Qian,, M. Inouye,, and M. Ikura. 1999. Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ. Nature Struct. Biol. 6:729734.
11. Varughese, K. I.,, Madhusudan, X., Z. Zhou,, J. M. Whiteley,, and J. A. Hock. 1998. Formation of a novel four-helix bundle and molecular recognition sites by dimerization of a response regulator phosphotransferase. Mol. Cell 2:485493.
12. Williams, S. B.,, and V. Stewart. 1999. Functional similarities among two-component sensors and methyl-accepting chemotaxis proteins suggest a role for linker region amphipathic helices in transmembrane signal transduction. Mol. Microbiol. 33:10931102.
13. Zapf, J. W.,, U. Sen,, Madhusudan,, J. A. Hoch,, and K. I. Varughese. 2000. A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction. Struct. Fold. Des. 8:851862.

Tables

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Table 1

Two-component systems regulating toxin production

Citation: Stibitz S. 2003. Two-Component Systems, p 3-24. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch1

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