A close-up view of the VraSR two-component system: A mediator of Staphylococcus aureus response to cell wall damage

Journal of Biological Chemistry

Volumn 283, Issue 18, 2008, Pages 12354-12364

  Belcheva, Antoaneta ^a   Golemi Kotra, Dasantila ^a  

^a YORK UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDES; BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; CHEMICAL REACTIONS; INTERNET; OLIGOMERS; PLANTS (BOTANY); SIGNAL TRANSDUCTION;

ACTIVE STATES; CELL WALLS; COMPONENT SYSTEMS; DEPHOSPHORYLATION; EFFECTOR DOMAINS; HISTIDINE PROTEIN KINASES; IN VITRO; MEDIATED SIGNALING PATHWAYS; MOLECULAR BASES; NOVEL STRATEGIES; OUTPUT RESPONSES; PEPTIDOGLYCAN; PHOSPHORYL GROUPS; REGULATORY DOMAINS; RESPONSE REGULATORS; S. AUREUS; SENSING CELLS; SIGNAL TRANSDUCTION MECHANISMS; STAPHYLOCOCCUS AUREUS; TARGET CELLS; VANCOMYCIN;

PHOSPHORYLATION;

DIMER; PEPTIDOGLYCAN; PROTEIN HISTIDINE KINASE; PROTEIN VRAR; PROTEIN VRAS; REGULATOR PROTEIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; DNA; DNA BINDING PROTEIN; HYBRID PROTEIN; MUTANT PROTEIN; PHOSPHOPROTEIN PHOSPHATASE; VRAR PROTEIN, STAPHYLOCOCCUS AUREUS; VRAS PROTEIN, STAPHYLOCOCCUS AUREUS;

AMINO ACID SEQUENCE; ARTICLE; AUTOPHOSPHORYLATION; BACTERIAL CELL WALL; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; MEMBRANE DAMAGE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEPHOSPHORYLATION; PROTEIN DNA BINDING; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; REGULATORY MECHANISM; SEQUENCE ANALYSIS; SIGNAL TRANSDUCTION; STAPHYLOCOCCUS AUREUS; CELL WALL; CHEMISTRY; ELECTROSPRAY MASS SPECTROMETRY; ENZYMOLOGY; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT;

STAPHYLOCOCCUS AUREUS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CELL WALL; DNA; DNA-BINDING PROTEINS; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; PHOSPHOPROTEIN PHOSPHATASES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; STAPHYLOCOCCUS AUREUS;

EID: 45549091606     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M710010200     Document Type: Article

References (45)

1. Kuroda, M., Kuwahara-Arai, K., and Hiramatsu, K. (2000) Biochem. Biophys. Res. Commun. 269, 485-490
2. Kuroda, M., Kuroda, H., Oshima, T., Takeuchi, F., Mori, H., and Hiramatsu, K. (2003) Mol. Microbiol. 49, 807-821
3. Boyle-Vavra, S., Yin, S., and Daum, R. S. (2006) FEMS Microbiol. Lett. 262, 163-171
4. Lukat, G. S., and Stock, J. B. (1993) J. Cell. Biochem. 51, 41-46
5. Kleerebezem, M., Quadri, L. E., Kuipers, O. P., and de Vos, W. M. (1997) Mol. Microbiol. 24, 895-904
6. Raivio, T. L., and Silhavy, T. J. (1997) J. Bacteriol. 179, 7724-7733
7. Mascher, T. (2006) FEMS Microbiol. Lett. 264, 133-144
8. West, A. H., and Stock, A. M. (2001) Trends Biochem. Sci. 26, 369-376
9. Robinson, V. L., Buckler, D. R., and Stock, A. M. (2000) Nat. Struct. Biol. 7, 626-633
10. Stock, A. M., Robinson, V. L., and Goudreau, P. N. (2000) Annu. Rev. Biochem. 69, 183-215
11. Gao, R., Mack, T. R., and Stock, A. M. (2007) Trends Biochem. Sci. 32, 225-234
12. Wright, G. D., Holman, T. R., and Walsh, C. T. (1993) Biochemistry 32, 5057-5063
13. Mascher, T., Margulis, N. G., Wang, T., Ye, R. W., and Helmann, J. D. (2003) Mol. Microbiol. 50, 1591-1604
14. Utaida, S., Dunman, P. M., Macapagal, D., Murphy, E., Projan, S. J., Singh, V. K., Jayaswal, R. K., and Wilkinson, B. J. (2003) Microbiology 149, 2719-2732
15. Sobral, R. G., Jones, A. E., Des Etages, S. G., Dougherty, T. J., Peitzsch, R. M., Gaasterland, T., Ludovice, A. M., de Lencastre, H., and Tomasz, A. (2007) J. Bacteriol. 189, 2376-2391
16. Gardete, S., Wu, S. W., Gill, S., and Tomasz, A. (2006) Antimicrob. Agents Chemother. 50, 3424-3434
17. Fan, X., Liu, Y., Smith, D., Konermann, L., Siu, K. W., and Golemi, D. (2007) J. Biol. Chem. 282, 35143-35152
18. Green, D. W. (2002) Expert Opin. Ther. Targets 6, 1-19
19. Fuda, C. C., Fisher, J. F., and Mobashery, S. (2005) Cell Mol. Life Sci. 62, 2617-2633
20. Walsh, C. (2003) Nat. Rev. Microbiol. 1, 65-70
21. Nathan, C. (2004) Nature 431, 899-902
22. Mwangi, M. M., Wu, S. W., Zhou, Y., Sieradzki, K., de Lencastre, H., Richardson, P., Bruce, D., Rubin, E., Myers, E., Siggia, E. D., and Tomasz, A. (2007) Proc. Natl. Acad. Sci. U. S. A. 104, 9451-9456
23. Stephenson, K., and Hoch, J. A. (2002) Curr. Opin. Pharmacol. 2, 507-512
24. Okada, A., Gotoh, Y., Watanabe, T., Furuta, E., Yamamoto, K., and Utsumi, R. (2007) Methods Enzymol. 422, 386-395
25. Stephenson, K., and Hoch, J. A. (2002) Curr. Drug Targets Infect. Disord. 2, 235-246
26. Ulijasz, A. T., Kay, B. K., and Weisblum, B. (2000) Biochemistry 39, 11417-11424
27. Janausch, I. G., Garcia-Moreno, I., and Unden, G. (2002) J. Biol. Chem. 277, 39809-39814
28. Kenney, L. J., Bauer, M. D., and Silhavy, T. J. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 8866-8870
29. Aiba, H., Nakasai, F., Mizushima, S., and Mizuno, T. (1989) J. Biochem. (Tokyo) 106, 5-7
30. Birkey, S. M., Liu, W., Zhang, X., Duggan, M. F., and Hulett, F. M. (1998) Mol. Microbiol. 30, 943-953
31. Roggiani, M., and Dubnau, D. (1993) J. Bacteriol. 175, 3182-3187
32. Zhang, J. H., Xiao, G., Gunsalus, R. P., and Hubbell, W. L. (2003) Biochemistry 42, 2552-2559
33. Qin, L., Yoshida, T., and Inouye, M. (2001) Proc. Natl. Acad. Sci. U. S. A. 98, 908-913
34. Ames, S. K., Frankema, N., and Kenney, L. J. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 11792-11797
35. Yamamoto, K., Hirao, K., Oshima, T., Aiba, H., Utsumi, R., and Ishihama, A. (2005) J. Biol. Chem. 280, 1448-1456
36. Skerker, J. M., Prasol, M. S., Perchuk, B. S., Biondi, E. G., and Laub, M. T. (2005) PLoS Biol. 3, e334
37. Kato, Y., Suzuki, T., Ida, T., Maebashi, K., Sakurai, M., Shiotani, J., and Hayashi, I. (2008) Int. J. Antimicrob. Agents 31, 64-70
38. McCleary, W. R., Stock, J. B., and Ninfa, A. J. (1993) J. Bacteriol. 175, 2793-2798
39. Eldridge, A. M., Kang, H. S., Johnson, E., Gunsalus, R., and Dahlquist, F. W. (2002) Biochemistry 41, 15173-15180
40. Birck, C., Malfois, M., Svergun, D., and Samama, J. (2002) J. Mol. Biol. 321, 447-457
41. Dyer, C. M., and Dahlquist, F. W. (2006) J. Bacteriol. 188, 7354-7363
42. Da Re, S., Schumacher, J., Rousseau, P., Fourment, J., Ebel, C., and Kahn, D. (1999) Mol. Microbiol. 34, 504-511
43. Bergstrom, L. C., Qin, L., Harlocker, S. L., Egger, L. A., and Inouye, M. (1998) Genes Cells 3, 777-788
44. Galinier, A., Garnerone, A. M., Reyrat, J. M., Kahn, D., Batut, J., and Boistard, P. (1994) J. Biol. Chem. 269, 23784-23789
45. Darwin, A. J., Li, J., and Stewart, V. (1996) Mol. Microbiol. 20, 621-632