Characterization of the cheY genes from Leptospira interrogans and their effects on the behavior of Escherichia coli

Biochemical and Biophysical Research Communications

Volumn 345, Issue 2, 2006, Pages 858-866

  Li, Zhen Hong ^a   Dong, Ke ^a   Yuan, Jian Ping ^a   Hu, Bao Yu ^a   Liu, Jing Xing ^a   Zhao, Guo Ping ^b   Guo, Xiao Kui ^a  

^a SHANGHAI JIAO TONG UNIVERSITY SCHOOL OF MEDICINE   (China)

^b CHINESE NATIONAL HUMAN GENOME CENTER AT SHANGHAI   (China)

Author keywords

Chemotaxis; cheY; L. interrogans

Indexed keywords

ASPARTIC ACID;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENOME; CHEMOTAXIS; CHEY GENE; CONTROLLED STUDY; ESCHERICHIA COLI; GENE; GENE OVEREXPRESSION; LEPTOSPIRA INTERROGANS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION;

AMINO ACID SEQUENCE; ASPARTIC ACID; BACTERIAL PROTEINS; BASE SEQUENCE; CHEMOTAXIS; CLONING, MOLECULAR; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, BACTERIAL; GENES, BACTERIAL; LEPTOSPIRA INTERROGANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PHOSPHOPROTEINS; SIGNAL TRANSDUCTION;

ESCHERICHIA COLI; LEPTOSPIRA INTERROGANS;

EID: 33646913537     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.04.159     Document Type: Article

References (35)

1. Faine S., Adler B., Bolin C., and Perolat P. Leptospira and Leptospirosis (1999), Medisci, Melbourne
2. Ren S.X., Fu G., Jiang X.G., Zeng R., Miao Y.G., Xu H., Zhang Y.X., Xiong H., Lu G., Lu L.F., Jiang H.Q., Jia J., Tu Y.F., Jiang J.X., Gu W.Y., Zhang Y.Q., Cai Z., Sheng H.H., Yin H.F., Zhang Y., Zhu G.F., Wan M., Huang H.L., Qian Z., Wang S.Y., Ma W., Yao Z.J., Shen Y., Qiang B.Q., Xia Q.C., Guo X.K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.M., Shi M.H., Chen Z., Xu J.G., and Zhao G.P. Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing. Nature 422 (2003) 888-893
3. Nascimento A.L., Verjovski-Almeida S., Van Sluys M.A., Monteiro-Vitorello C.B., Camargo L.E., Digiampietri L.A., Harstkeerl R.A., Ho P.L., Marques M.V., Oliveira M.C., Setubal J.C., Haake D.A., and Martins E.A. Genome features of Leptospira interrogans serovar Copenhageni. Braz. J. Med. Biol. Res. 37 (2004) 459-477
4. Nixon B.T., Ronson C.W., and Ausubel F.M. Two-component regulatory systems responsive to environmental stimuli share strongly conserved domains with the nitrogen assimilation regulatory genes ntrB and ntrC. Proc. Natl. Acad. Sci. USA 83 (1986) 7850-7854
5. Ronson C.W., Nixon B.T., and Ausubel F.M. Conserved domains in bacterial regulatory proteins that respond to environmental stimuli. Cell 49 (1987) 579-581
6. Bourret R.B., Hess J.F., Borkovich K.A., Pakula A.A., and Simon M.I. Protein phosphorylation in chemotaxis and two-component regulatory systems of bacteria. J. Biol. Chem. 264 (1989) 7085-7088
7. Charon N.W., and Goldstein S.F. Genetics of motility and chemotaxis of a fascinating group of bacteria: the spirochetes. Annu. Rev. Genet. 36 (2002) 47-73
8. Yuri K., Takamoto Y., Okada M., Hiramune T., Kikuchi N., and Yanagawa R. Chemotaxis of leptospires to hemoglobin in relation to virulence. Infect. Immun. 61 (1993) 2270-2272
9. Parkinson J.S. Bacterial chemotaxis: a new player in response regulator dephosphorylation. J. Bacteriol. 185 (2003) 1492-1494
10. Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R., Lathigra R., White O., Ketchum K.A., Dodson R., Hickey E.K., Gwinn M., Dougherty B., Tomb J.F., Fleischmann R.D., Richardson D., Peterson J., Kerlavage A.R., Quackenbush J., Salzberg S., Hanson M., van Vugt R., Palmer N., Adams M.D., Gocayne J., Weidman J., Utterback T., Watthey L., McDonald L., Artiach P., Bowman C., Garland S., Fuji C., Cotton M.D., Horst K., Roberts K., Hatch B., Smith H.O., and Venter J.C. Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi. Nature 390 (1997) 580-586
11. Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., Dodson R., Gwinn M., Hickey E.K., Clayton R., Ketchum K.A., Sodergren E., Hardham J.M., McLeod M.P., Salzberg S., Peterson J., Khalak H., Richardson D., Howell J.K., Chidambaram M., Utterback T., McDonald L., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S., Hatch B., Horst K., Roberts K., Sandusky M., Weidman J., Smith H.O., and Venter J.C. Complete genome sequence of Treponema pallidum, the syphilis spirochete. Science 281 (1998) 375-388
12. Greck M., Platzer J., Sourjik V., and Schmitt R. Analysis of a chemotaxis operon in Rhizobium meliloti. Mol. Microbiol. 15 (1995) 989-1000
13. Li Z.H., Dong K., Sun J.C., Yuan J.P., Hu B.Y., Liu J.X., Zhao G.P., and Guo X.K. Characterization of cheW genes of Leptospira interrogans and their effects in Escherichia coli. Acta Biochim. Biophys. Sin. (Shanghai) 38 (2006) 79-88
14. Sanders D.A., Gillece-Castro B.L., Stock A.M., Burlingame A.L., and Koshland Jr. D.E. Identification of the site of phosphorylation of the chemotaxis response regulator protein, CheY. J. Biol. Chem. 264 (1989) 21770-21778
15. Bourret R.B., Hess J.F., and Simon M.I. Conserved aspartate residues and phosphorylation in signal transduction by the chemotaxis protein CheY. Proc. Natl. Acad. Sci. USA 87 (1990) 41-45
16. Barak R., and Eisenbach M. Correlation between phosphorylation of the chemotaxis protein CheY and its activity at the flagellar motor. Biochemistry 31 (1992) 1821-1826
17. Welch M., Oosawa K., Aizawa S., and Eisenbach M. Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria. Proc. Natl. Acad. Sci. USA 90 (1993) 8787-8791
18. Wolfe A.J., and Berg H.C. Migration of bacteria in semisolid agar. Proc. Natl. Acad. Sci. USA 86 (1989) 6973-6977
19. Segall J.E., Ishihara A., and Berg H.C. Chemotactic signaling in filamentous cells of Escherichia coli. J. Bacteriol. 161 (1985) 51-59
20. Parkinson J.S. Complementation analysis and deletion mapping of Escherichia coli mutants defective in chemotaxis. J. Bacteriol. 135 (1978) 45-53
21. Lukat G.S., Lee B.H., Mottonen J.M., Stock A.M., and Stock J.B. Roles of the highly conserved aspartate and lysine residues in the response regulator of bacterial chemotaxis. J. Biol. Chem. 266 (1991) 8348-8354
22. Borkovich K.A., Kaplan N., Hess J.F., and Simon M.I. Transmembrane signal transduction in bacterial chemotaxis involves ligand-dependent activation of phosphate group transfer. Proc. Natl. Acad. Sci. USA 86 (1989) 1208-1212
23. Hess J.F., Oosawa K., Matsumura P., and Simon M.I. Protein phosphorylation is involved in bacterial chemotaxis. Proc. Natl. Acad. Sci. USA 84 (1987) 7609-7613
24. Hess J.F., Oosawa K., Kaplan N., and Simon M.I. Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis. Cell 53 (1988) 79-87
25. Stock A., Koshland Jr. D.E., and Stock J. Homologies between the Salmonella typhimurium CheY protein and proteins involved in the regulation of chemotaxis, membrane protein synthesis, and sporulation. Proc. Natl. Acad. Sci. USA 82 (1985) 7989-7993
26. Stock A.M., Mottonen J.M., Stock J.B., and Schutt C.E. Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis. Nature 337 (1989) 745-749
27. Stock A.M., Wylie D.C., Mottonen J.M., Lupas A.N., Ninfa E.G., Ninfa A.J., Schutt C.E., and Stock J.B. Phosphoproteins involved in bacterial signal transduction. Cold Spring Harb. Symp. Quant. Biol. 53 Pt 1 (1988) 49-57
28. Volz K., and Matsumura P. Crystal structure of Escherichia coli CheY refined at 1.7-A resolution. J. Biol. Chem. 266 (1991) 15511-15519
29. Silversmith R.E. High mobility of carboxyl-terminal region of bacterial chemotaxis phosphatase CheZ is diminished upon binding divalent cation or CheY-P substrate. Biochemistry 44 (2005) 7768-7776
30. Shukla D., and Matsumura P. Mutations leading to altered CheA binding cluster on a face of CheY. J. Biol. Chem. 270 (1995) 24414-24419
31. Roman S.J., Meyers M., Volz K., and Matsumura P. A chemotactic signaling surface on CheY defined by suppressors of flagellar switch mutations. J. Bacteriol. 174 (1992) 6247-6255
32. Sanna M.G., and Simon M.I. Isolation and in vitro characterization of CheZ suppressors for the Escherichia coli chemotactic response regulator mutant CheYN23D. J. Biol. Chem. 271 (1996) 7357-7361
33. Sanna M.G., Swanson R.V., Bourret R.B., and Simon M.I. Mutations in the chemotactic response regulator, CheY, that confer resistance to the phosphatase activity of CheZ. Mol. Microbiol. 15 (1995) 1069-1079
34. Bellsolell L., Cronet P., Majolero M., Serrano L., and Coll M. The three-dimensional structure of two mutants of the signal transduction protein CheY suggest its molecular activation mechanism. J. Mol. Biol. 257 (1996) 116-128
35. McEvoy M.M., Hausrath A.C., Randolph G.B., Remington S.J., and Dahlquist F.W. Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway. Proc. Natl. Acad. Sci. USA 95 (1998) 7333-7338