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. 1995 Jul;177(13):3894–3896. doi: 10.1128/jb.177.13.3894-3896.1995

A study of the double mutation of dnaJ and cbpA, whose gene products function as molecular chaperones in Escherichia coli.

C Ueguchi 1, T Shiozawa 1, M Kakeda 1, H Yamada 1, T Mizuno 1
PMCID: PMC177114  PMID: 7601860

Abstract

The CbpA protein is an analog of the DnaJ molecular chaperone of Escherichia coli. To gain insight into the function of CbpA, we examined the nature of a cbpA null mutation with special reference to those of dnaK and dnaJ null mutations. In particular, the cbpA dnaJ double-null mutant was found to exhibit severe defects in cell growth, namely, a very narrow temperature range for growth, a defect in cell division, and susceptibility to killing by carbon starvation. These phenotypes are very similar to those reported for dnaK null mutants but not to those of dnaJ null mutants. Our results are best interpreted by assuming that CbpA is capable of compensating for DnaJ for cell growth and thus that the function(s) of CbpA is closely related to that of DnaJ.

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Selected References

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  1. Bukau B., Walker G. C. Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism. J Bacteriol. 1989 May;171(5):2337–2346. doi: 10.1128/jb.171.5.2337-2346.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Ellis R. J., van der Vies S. M. Molecular chaperones. Annu Rev Biochem. 1991;60:321–347. doi: 10.1146/annurev.bi.60.070191.001541. [DOI] [PubMed] [Google Scholar]
  3. Georgopoulos C. The emergence of the chaperone machines. Trends Biochem Sci. 1992 Aug;17(8):295–299. doi: 10.1016/0968-0004(92)90439-g. [DOI] [PubMed] [Google Scholar]
  4. Grossman A. D., Erickson J. W., Gross C. A. The htpR gene product of E. coli is a sigma factor for heat-shock promoters. Cell. 1984 Sep;38(2):383–390. doi: 10.1016/0092-8674(84)90493-8. [DOI] [PubMed] [Google Scholar]
  5. Kawasaki Y., Wada C., Yura T. Roles of Escherichia coli heat shock proteins DnaK, DnaJ and GrpE in mini-F plasmid replication. Mol Gen Genet. 1990 Jan;220(2):277–282. doi: 10.1007/BF00260494. [DOI] [PubMed] [Google Scholar]
  6. Liberek K., Marszalek J., Ang D., Georgopoulos C., Zylicz M. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2874–2878. doi: 10.1073/pnas.88.7.2874. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. McCarty J. S., Walker G. C. DnaK mutants defective in ATPase activity are defective in negative regulation of the heat shock response: expression of mutant DnaK proteins results in filamentation. J Bacteriol. 1994 Feb;176(3):764–780. doi: 10.1128/jb.176.3.764-780.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Sell S. M., Eisen C., Ang D., Zylicz M., Georgopoulos C. Isolation and characterization of dnaJ null mutants of Escherichia coli. J Bacteriol. 1990 Sep;172(9):4827–4835. doi: 10.1128/jb.172.9.4827-4835.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Silver P. A., Way J. C. Eukaryotic DnaJ homologs and the specificity of Hsp70 activity. Cell. 1993 Jul 16;74(1):5–6. doi: 10.1016/0092-8674(93)90287-z. [DOI] [PubMed] [Google Scholar]
  10. Spence J., Cegielska A., Georgopoulos C. Role of Escherichia coli heat shock proteins DnaK and HtpG (C62.5) in response to nutritional deprivation. J Bacteriol. 1990 Dec;172(12):7157–7166. doi: 10.1128/jb.172.12.7157-7166.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Tilly K., McKittrick N., Zylicz M., Georgopoulos C. The dnaK protein modulates the heat-shock response of Escherichia coli. Cell. 1983 Sep;34(2):641–646. doi: 10.1016/0092-8674(83)90396-3. [DOI] [PubMed] [Google Scholar]
  12. Tilly K., Yarmolinsky M. Participation of Escherichia coli heat shock proteins DnaJ, DnaK, and GrpE in P1 plasmid replication. J Bacteriol. 1989 Nov;171(11):6025–6029. doi: 10.1128/jb.171.11.6025-6029.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Ueguchi C., Kakeda M., Yamada H., Mizuno T. An analogue of the DnaJ molecular chaperone in Escherichia coli. Proc Natl Acad Sci U S A. 1994 Feb 1;91(3):1054–1058. doi: 10.1073/pnas.91.3.1054. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Wild J., Altman E., Yura T., Gross C. A. DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli. Genes Dev. 1992 Jul;6(7):1165–1172. doi: 10.1101/gad.6.7.1165. [DOI] [PubMed] [Google Scholar]
  15. Yamashino T., Kakeda M., Ueguchi C., Mizuno T. An analogue of the DnaJ molecular chaperone whose expression is controlled by sigma s during the stationary phase and phosphate starvation in Escherichia coli. Mol Microbiol. 1994 Aug;13(3):475–483. doi: 10.1111/j.1365-2958.1994.tb00442.x. [DOI] [PubMed] [Google Scholar]
  16. Zylicz M., Ang D., Liberek K., Georgopoulos C. Initiation of lambda DNA replication with purified host- and bacteriophage-encoded proteins: the role of the dnaK, dnaJ and grpE heat shock proteins. EMBO J. 1989 May;8(5):1601–1608. doi: 10.1002/j.1460-2075.1989.tb03544.x. [DOI] [PMC free article] [PubMed] [Google Scholar]

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