Identification of the Vibrio vulnificus htpG gene and its influence on cold shock recovery (Journal of Microbiology, 50, 4, (2012), 707-711, 10.1007/s12275-012-2294-z);Identification of the Vibrio vulnificus htpG gene and its influence on cold shock recovery

Journal of Microbiology

Volumn 50, Issue 4, 2012, Pages 707-711

  Choi, Slae ^a   Jang, Kyungku ^a   Choi, Seulah ^b   Yun, Hee jee ^b   Kang, Dong Hyun ^a  

^a Seoul National University   (South Korea)

^b Hankuk University of Foreign Studies   (South Korea)

Author keywords

chaperone; cold shock; heat shock protein; V. vulnificus htpG

Indexed keywords

ESCHERICHIA COLI; VIBRIO VULNIFICUS;

EID: 84865801441     PISSN: 12258873     EISSN: 19763794     Source Type: Journal    
DOI: 10.1007/s12275-015-0740-4     Document Type: Erratum

References (29)

1. Bardwell, J. C. A. and Craig, E. A. 1987. Eukaryotic Mr 83, 000 heat shock protein has a homologue in Escherichia coli. Proc. Natl. Acad. Sci. USA84, 5177-5181.
2. Bardwell, J. C. A. and Craig, E. A. 1988. Ancient heat shock protein is dispensable. J. Bacteriol. 172, 6042-6047.
3. Borkovich, K. A., Farrelly, F. W., Finkelstein, D. B., Taulien, J., and Lindquist, S. 1989. Hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol. Cell Biol. 9, 3919-3930.
4. Genest, O., Hoskins, J. R., Camberg, J. L., Doyle, S. M., and Wickner, S. 2011. Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling. Proc. Natl. Acad. Sci. USA108, 8206-8211.
5. Goldstein, J., Pollitt, N. S., and Inouye, M. 1990. Major cold-shock protein of Escherichia coli. Proc. Natl. Acad. Sci. USA 87, 283-287.
6. Guisbert, E., Yura, T., Rhodius, V. A., and Gross C. A. 2008. Convergence of molecular, modeling, and systems approaches for an understanding of the Escherichia coli heat shock response. Microbiol. Mol. Biol. Rev. 72, 545-554.
7. Hessling, M., Richter, K., and Buchner, J. 2009. Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90. Nat. Struct. Mol. Biol. 16, 287-293.
8. Jeong, H. S., Kim, S. M., Lim, M. S., Kim, K. S., and Choi, S. H. 2010 Direct interaction between quorum sensing regulator SmcR and RNAP is mediated by IHF to activate vvpE encoding elastase in Vibrio vulnificus. J. Biol. Chem. 285, 9357-9366.
9. Jiang, W., Fang, L., and Inouye, M. 1996. The role of the 5-end untranslated region of the mRNA for CspA, the major cold-shock protein of Escherichia coli. J. Bacteriol. 178, 4919-4925.
10. Jones, M. K. and Oliver, J. D. 2009. Vibrio vulnificus: Disease and pathogenesis. Infect. Immun. 77, 1723-1733.
11. Kim, B. S., Hwang, J. W., Kim, M. H., and Choi, S. H. 2011. Cooperative regulation of the Vibrio vulnificus nan cluster by NanR, cAMP receptor protein, and N-acetylmannosamine-6-phosphate. J. Biol. Chem. 286, 40889-40899.
12. Larsen, R. A., Wilson, M. M., Guss, A. M., and Metcalf, W. W. 2002. Genetic analysis of pigment biosynthesis in Xanthobacter autotrophicus Py2 using a new, highly efficient transposon mutagenesis system that is functional in a wide variety of bacteria. Arch. Microbiol. 178, 193-201.
13. Meyer, A. S. and Baker, T. A. 2011. Proteolysis in the Escherichia coli heat shock response: a player at many levels. Curr. Opin. Microbiol. 14, 194-199.
14. Miller, V. L. and Mekalanos, J. J. 1988. A novel suicide vector and its use in construction of insertion mutations: osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR. J. Bacteriol. 170, 2575-2583.
15. Milton, D. L., O'Toole, R., Horstedt, P., and Wolf-Watz, H. 1996. Flagellin A is essential for the virulence of Vibrio anguillarum. J. Bacteriol. 178, 1310-1319.
16. Motojima-Miyazaki, Y., Yoshida, M., and Motojima, F. 2010. Ribosomal protein L2 associates with E. coli HtpG and activates its ATPase activity. Biochem. Biophys. Res. Commun. 400, 241-245.
17. Murphy, K. C., Campellone, K. G., and Poteete, A. R. 2000. PCR-mediated gene replacement in Escherichia coli. Gene246, 321-330.
18. Phadtare, S. and Severinov, K. 2010. RNA remodeling and gene regulation by cold shock proteins. RNA Biol. 7, 788-795.
19. Picard, D. 2002. Heat-shock protein 90, a chaperone for folding and regulation. Cell Mol. Life Sci. 59, 1640-1648.
20. Sambrook, J. and Russell, D. W. 2001. Molecular Cloning: A Laboratory Manual, 3rd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, N. Y., USA.
21. Sato, T., Minagawa, S., Kojima, E., Okamoto, N., and Nakamoto, H. 2010. HtpG, the prokaryotic homologue of Hsp90, stabilizes a phycobilisome protein in the cyanobacterium Synechococcus elongatus PCC 7942. Mol. Microbiol. 76, 576-589.
22. Shiau, A. K., Harris, S. F., Southworth, D. R., and Agard, D. A. 2006. Structural analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell127, 329-340.
23. Simon, R., Priefer, U., and Pulher, A. 1983. A broad host range mobilisation system for in vivo genetic engineering: transposon mutagenesis in Gram-negative bacteria. Bio/Technology1, 784-791.
24. Taipale, M., Jarosz, D. F., and Lindquist, S. 2010. HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat. Rev. Mol. Cell Biol. 11, 515-528.
25. Thomas, J. G. and Baneyx, F. 2000. ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells. Mol. Microbiol. 36, 1360-1370.
26. Wandinger, S. K., Richter, K., and Buchner, J. 2008. The Hsp90 chaperone machinery. J. Biol. Chem. 283, 18473-18477.
27. Weber, M. H. and Marahiel, M. A. 2003. Bacterial cold shock responses. Sci Prog. 86, 9-75.
28. Wood, R. R. and Arias, C. R. 2011. Evaluation of global gene expression during cold shock in the human pathogen Vibrio vulnificus. Mar. Biotechnol. 13, 942-954.
29. Yura, T. and Nakahigashi, K. 1999. Regulation of the heat-shock response. Curr. Opin. Microbiol. 2, 153-158.