CheV: CheW-like coupling proteins at the core of the chemotaxis signaling network

Trends in Microbiology

Volumn 18, Issue 11, 2010, Pages 494-503

  Alexander, Roger P ^a   Lowenthal, Andrew C ^b   Harshey, Rasika M ^c   Ottemann, Karen M ^b  

^a YALE UNIVERSITY   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF TEXAS AT AUSTIN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CHEA KINASE; CHEW PROTEIN; PHOSPHATE; PROTEIN CHEV; UNCLASSIFIED DRUG;

ADAPTATION; AMINO ACID SEQUENCE; CHEMORECEPTOR; CHEMOTAXIS; CONFORMATIONAL TRANSITION; GENE MUTATION; NONHUMAN; PHYLOGENY; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW; SIGNAL TRANSDUCTION;

BACTERIA; BACTERIAL PROTEINS; CHEMOTACTIC FACTORS; CHEMOTAXIS; PHOSPHORYLATION; SIGNAL TRANSDUCTION;

BACTERIA (MICROORGANISMS);

EID: 77958188709     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tim.2010.07.004     Document Type: Review

References (71)

1. Wadhams G.H., Armitage J.P. Making sense of it all: bacterial chemotaxis. Nat. Rev. Mol. Cell Biol. 2004, 5:1024-1037.
2. Miller L.D., et al. Diversity in bacterial chemotactic responses and niche adaptation. Adv. Appl. Microbiol. 2009, 66:53-75.
3. Baker M.D., et al. Signal transduction in bacterial chemotaxis. Bioessays 2006, 28:9-22.
4. Hazelbauer G.L., et al. Bacterial chemoreceptors: high-performance signaling in networked arrays. Trends Biochem. Sci. 2008, 33:9-19.
5. Bray D. Bacterial chemotaxis and the question of gain. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:7-9.
6. Zeke A., et al. Scaffolds: interaction platforms for cellular signalling circuits. Trends Cell Biol. 2009, 19:364-374.
7. Shaw A.S., Filbert E.L. Scaffold proteins and immune-cell signalling. Nat. Rev. Immunol. 2009, 9:47-56.
8. Dohlman H.G. A scaffold makes the switch. Sci. Signal. 2008, 1:pe46.
9. Stewart R.C. Protein histidine kinases: assembly of active sites and their regulation in signaling pathways. Curr. Opin. Microbiol. 2010, 13:133-141.
10. Sarkar M.K., et al. Chemotaxis signaling protein CheY binds to the rotor protein FliN to control the direction of flagellar rotation in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:9370-9375.
11. Silversmith R.E. Auxiliary phosphatases in two-component signal transduction. Curr. Opin. Microbiol. 2010, 13:177-183.
12. Szurmant H., Ordal G.W. Diversity in chemotaxis mechanisms among the bacteria and archaea. Microbiol. Mol. Biol. Rev. 2004, 68:301-319.
13. Wuichet K., et al. Comparative genomic and protein sequence analysis of a complex system controlling bacterial chemotaxis. Methods Enzymol. 2007, 422:1-31.
14. Kirby J.R. Chemotaxis-like regulatory systems: unique roles in diverse bacteria. Annu. Rev. Microbiol. 2009, 63:45-59.
15. Fredrick K.L., Helmann J.D. Dual chemotaxis signaling pathways in Bacillus subtilis: A sigma-D-dependent gene encodes a novel protein with both CheW and CheY homologous domains. J. Bacteriol. 1994, 176:2727-2735.
16. Rosario M.M., et al. Chemotaxis in Bacillus subtilis requires either of two functionally redundant CheW homologs. J. Bacteriol. 1994, 176:2736-2739.
17. Borkovich K.A., et al. Transmembrane signal transduction in bacterial chemotaxis involves ligand-dependent activation of phosphate group transfer. Proc. Natl. Acad. Sci. U. S. A. 1989, 86:1208-1212.
18. Gegner J.A., et al. Assembly of an MCP receptor, CheW, and kinase CheA complex in the bacterial chemotaxis signal transduction pathway. Cell 1992, 70:975-982.
19. Lowenthal A.C., et al. A fixed-time diffusion analysis method determines that the three cheV genes of Helicobacter pylori differentially affect motility. Microbiology 2009, 155:1181-1191.
20. Bourret R.B. Receiver domain structure and function in response regulator proteins. Curr. Opin. Microbiol. 2010, 13:142-149.
21. Gao R., Stock A.M. Biological insights from structures of two-component proteins. Annu. Rev. Microbiol. 2009, 63:133-154.
22. Gao R., et al. Bacterial response regulators: versatile regulatory strategies from common domains. Trends Biochem. Sci. 2007, 32:225-234.
23. Boukhvalova M.S., et al. CheW binding interactions with CheA and Tar. Importance for chemotaxis signaling in Escherichia coli. J. Biol. Chem. 2002, 277:22251-22259.
24. Erbse A., Falke J. The core signaling proteins of bacterial chemotaxis assemble to form an ultrastable complex. Biochemistry 2009, 48:6975-6987.
25. Schulmeister S., et al. Protein. exchange dynamics at chemoreceptor clusters in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:6403-6408.
26. Kim S.H., et al. Dynamic and clustering model of bacterial chemotaxis receptors: structural basis for signaling and high sensitivity. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:11611-11615.
27. Boukhvalova M., et al. CheA kinase and chemoreceptor interaction surfaces on CheW. J. Biol. Chem. 2002, 277:23596-23603.
28. Liu J.D., Parkinson J.S. Genetic evidence for interaction between the CheW and Tsr proteins during chemoreceptor signaling by Escherichia coli. J. Bacteriol. 1991, 173:4941-4951.
29. Park S.Y., et al. Reconstruction of the chemotaxis receptor-kinase assembly. Nat. Struct. Mol. Biol. 2006, 13:400-407.
30. Kentner D., et al. Determinants of chemoreceptor cluster formation in Escherichia coli. Mol. Microbiol. 2006, 61:407-417.
31. Studdert C.A., Parkinson J.S. Insights into the organization and dynamics of bacterial chemoreceptor clusters through in vivo crosslinking studies. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:15623-15628.
32. Maddock J.R., Shapiro L. Polar location of the chemoreceptor complex in the Escherichia coli cell. Science 1993, 259:1717-1723.
33. Lamanna A.C., et al. Large increases in attractant concentration disrupt the polar localization of bacterial chemoreceptors. Mol. Microbiol. 2005, 57:774-785.
34. Galperin M.Y. Diversity of structure and function of response regulator output domains. Curr. Opin. Microbiol. 2010, 13:150-159.
35. Gao R., Stock A.M. Molecular strategies for phosphorylation-mediated regulation of response regulator activity. Curr. Opin. Microbiol. 2010, 13:160-167.
36. Jimenez-Pearson M.A., et al. Phosphate flow in the chemotactic response system of Helicobacter pylori. Microbiology 2005, 151:3299-3311.
37. Pittman M.S., et al. Chemotaxis in the human gastric pathogen Helicobacter pylori: different roles for CheW and the three CheV paralogues, and evidence for CheV2 phosphorylation. Microbiology 2001, 147:2493-2504.
38. Karatan E., et al. Phosphorylation of the response regulator CheV is required for adaptation to attractants during Bacillus subtilis chemotaxis. J. Biol. Chem. 2001, 276:43618-43626.
39. Frye J., et al. Identification of new flagellar genes of Salmonella enterica serovar Typhimurium. J. Bacteriol. 2006, 188:2233-2243.
40. Wang Q., et al. Uncovering a large set of genes that affect surface motility in Salmonella enterica serovar Typhimurium. J. Bacteriol. 2006, 188:7981-7984.
41. Terry K., et al. Chemotaxis plays multiple roles in Helicobacter pylori animal infection. Infect. Immun. 2005, 73:803-811.
42. Wang Q., et al. Gene. expression patterns during swarming in Salmonella typhimurium: genes specific to surface growth and putative new motility and pathogenicity genes. Mol. Microbiol. 2004, 52:169-187.
43. Sanders D.A., et al. Role of the CheW protein in bacterial chemotaxis: overexpression is equivalent to absence. J. Bacteriol. 1989, 171:6271-6278.
44. Garrity L.F., Ordal G.W. Activation of the CheA kinase by asparagine in Bacillus subtilis chemotaxis. Microbiology 1997, 143:2945-2951.
45. Hartley-Tassell L.E., et al. Identification and characterization of the aspartate chemosensory receptor of Campylobacter jejuni. Mol. Microbiol. 2009, 75:710-730.
46. Sourjik V., Schmitt R. Phosphotransfer between CheA, CheY1, and CheY2 in the chemotaxis signal transduction chain of Rhizobium meliloti. Biochemistry 1998, 37:2327-2335.
47. Stewart R.C. Activating and inhibitory mutations in the regulatory domain of CheB, the methylesterase in bacterial chemotaxis. J. Biol. Chem. 1993, 268:1921-1930.
48. Hess J.F., et al. Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis. Cell 1988, 53:79-87.
49. Thomas S.A., et al. Two variable active site residues modulate response regulator phosphoryl group stability. Mol. Microbiol. 2008, 69:453-465.
50. Rao C.V., Ordal G.W. The molecular basis of excitation and adaptation during chemotactic sensory transduction in bacteria. Contrib. Microbiol. 2009, 16:33-64.
51. Stock J., et al. Neither methylating nor demethylating enzymes are required for bacterial chemotaxis. Cell 1985, 42:683-690.
52. Estacio W., et al. Dual promoters are responsible for transcription initiation of the fla/che operon in Bacillus subtilis. J. Bacteriol. 1998, 180:3548-3555.
53. Prouty M.G., et al. The novel sigma54- and sigma28-dependent flagellar gene transcription hierarchy of Vibrio cholerae. Mol. Microbiol. 2001, 39:1595-1609.
54. Gosink K.K., et al. Analyses of the roles of the three cheA homologs in chemotaxis of Vibrio cholerae. J. Bacteriol. 2002, 184:1767-1771.
55. Tomb J.-F., et al. The complete genome sequence of the gastric pathogen Helicobacter pylori. Nature 1997, 388:539-547.
56. Sharma C.M., et al. The primary transcriptome of the major human pathogen Helicobacter pylori. Nature 2010, 464:250-255.
57. Ernst F.D., et al. Transcriptional profiling of Helicobacter pylori Fur- and iron-regulated gene expression. Microbiology 2005, 151:533-546.
58. Blackhart B.D., Zusman D.R. " Frizzy" genes of Myxococcus xanthus are involved in control of frequency of reversal of gliding motility. Proc. Natl. Acad. Sci. U. S. A. 1985, 82:8767-8770.
59. Martin A.C., et al. The roles of the multiple CheW and CheA homologues in chemotaxis and in chemoreceptor localization in Rhodobacter sphaeroides. Mol. Microbiol. 2001, 40:1261-1272.
60. Yao W., et al. Crystal structure of scaffolding protein CheW from Thermoanaerobacter tengcongensis. Biochem. Biophys. Res. Commun. 2007, 361:1027-1032.
61. Li Y., et al. Solution structure of the bacterial chemotaxis adaptor protein CheW from Escherichia coli. Biochem. Biophys. Res. Commun. 2007, 360:863-867.
62. Griswold I.J., et al. The solution structure and interactions of CheW from Thermotoga maritima. Nat. Struct. Biol. 2002, 9:121-125.
63. Cardozo M.J., et al. Disruption of chemoreceptor signaling arrays by high level of CheW, the receptor-kinase coupling protein. Mol. Microbiol. 2010, 75:1171-1181.
64. Borkovich K.A., Simon M.I. The dynamics of protein phosphorylation in bacterial chemotaxis. Cell 1990, 63:1339-1348.
65. Chalah A., Weis R.M. Site-specific and synergistic stimulation of methylation on the bacterial chemotaxis receptor Tsr by serine and CheW. BMC Microbiol. 2005, 5:12.
66. Marchant J., et al. Exploiting genome sequence: predictions for mechanisms of Campylobacter chemotaxis. Trends Microbiol. 2002, 10:155-159.
67. Dehal P.S., et al. MicrobesOnline: an integrated portal for comparative and functional genomics. Nucleic. Acids Res. 2009, 38:D396-400.
68. Tamura K., et al. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 2007, 24:1596-1599.
69. Thompson J.D., et al. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic. Acids Res. 1994, 22:4673-4680.
70. Schwede T., et al. SWISS-MODEL: an automated protein homology-modeling server. Nucleic. Acids Res. 2003, 31:3381-3385.
71. Edgar R.C. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic. Acids Res. 2004, 32:1792-1797.