This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Thomas, J. G.
Right arrow Articles by Baneyx, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Thomas, J. G.
Right arrow Articles by Baneyx, F.

 Previous Article  |  Next Article 

Journal of Bacteriology, October 1998, p. 5165-5172, Vol. 180, No. 19
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Roles of the Escherichia coli Small Heat Shock Proteins IbpA and IbpB in Thermal Stress Management: Comparison with ClpA, ClpB, and HtpG In Vivo

Jeffrey G. Thomasdagger and François Baneyx*

Department of Chemical Engineering, University of Washington, Seattle, Washington 98195

Received 24 April 1998/Accepted 30 July 1998

We have constructed an Escherichia coli strain lacking the small heat shock proteins IbpA and IbpB and compared its growth and viability at high temperatures to those of isogenic cells containing null mutations in the clpA, clpB, or htpG gene. All mutants exhibited growth defects at 46°C, but not at lower temperatures. However, the clpA, htpG, and ibp null mutations did not reduce cell viability at 50°C. When cultures were allowed to recover from transient exposure to 50°C, all mutations except Delta ibp led to suboptimal growth as the recovery temperature was raised. Deletion of the heat shock genes clpB and htpG resulted in growth defects at 42°C when combined with the dnaK756 or groES30 alleles, while the Delta ibp mutation had a detrimental effect only on the growth of dnaK756 mutants. Neither the overexpression of these heat shock proteins nor that of ClpA could restore the growth of dnaK756 or groES30 cells at high temperatures. Whereas increased levels of host protein aggregation were observed in dnaK756 and groES30 mutants at 46°C compared to wild-type cells, none of the null mutations had a similar effect. These results show that the highly conserved E. coli small heat shock proteins are dispensable and that their deletion results in only modest effects on growth and viability at high temperatures. Our data also suggest that ClpB, HtpG, and IbpA and -B cooperate with the major E. coli chaperone systems in vivo.

* Corresponding author. Mailing address: Department of Chemical Engineering, University of Washington, Box 351750, Seattle, WA 98195. Phone: (206) 685-7659. Fax: (206) 685-3451. E-mail: baneyx{at}cheme.washington.edu.

dagger Present address: Department of Chemical Engineering, University of Texas, Austin, TX 78712.

Journal of Bacteriology, October 1998, p. 5165-5172, Vol. 180, No. 19
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Nobre, L. S., Al-Shahrour, F., Dopazo, J., Saraiva, L. M. (2009). Exploring the antimicrobial action of a carbon monoxide-releasing compound through whole-genome transcription profiling of Escherichia coli. Microbiology 155: 813-824 [Abstract] [Full Text]  
  • Capestany, C. A., Tribble, G. D., Maeda, K., Demuth, D. R., Lamont, R. J. (2008). Role of the Clp System in Stress Tolerance, Biofilm Formation, and Intracellular Invasion in Porphyromonas gingivalis. J. Bacteriol. 190: 1436-1446 [Abstract] [Full Text]  
  • Malone, A. S., Chung, Y.-K., Yousef, A. E. (2006). Genes of Escherichia coli O157:H7 That Are Involved in High-Pressure Resistance. Appl. Environ. Microbiol. 72: 2661-2671 [Abstract] [Full Text]  
  • Ren, D., Zuo, R., Gonzalez Barrios, A. F., Bedzyk, L. A., Eldridge, G. R., Pasmore, M. E., Wood, T. K. (2005). Differential Gene Expression for Investigation of Escherichia coli Biofilm Inhibition by Plant Extract Ursolic Acid. Appl. Environ. Microbiol. 71: 4022-4034 [Abstract] [Full Text]  
  • Lizewski, S. E., Schurr, J. R., Jackson, D. W., Frisk, A., Carterson, A. J., Schurr, M. J. (2004). Identification of AlgR-Regulated Genes in Pseudomonas aeruginosa by Use of Microarray Analysis. J. Bacteriol. 186: 5672-5684 [Abstract] [Full Text]  
  • Laskowska, E., Bohdanowicz, J., Kuczynska-Wisnik, D., Matuszewska, E., Kedzierska, S., Taylor, A. (2004). Aggregation of heat-shock-denatured, endogenous proteins and distribution of the IbpA/B and Fda marker-proteins in Escherichia coli WT and grpE280 cells. Microbiology 150: 247-259 [Abstract] [Full Text]  
  • Tomoyasu, T., Takaya, A., Sasaki, T., Nagase, T., Kikuno, R., Morioka, M., Yamamoto, T. (2003). A New Heat Shock Gene, agsA, Which Encodes a Small Chaperone Involved in Suppressing Protein Aggregation in Salmonella enterica Serovar Typhimurium. J. Bacteriol. 185: 6331-6339 [Abstract] [Full Text]  
  • Weibezahn, J., Schlieker, C., Bukau, B., Mogk, A. (2003). Characterization of a Trap Mutant of the AAA+ Chaperone ClpB. J. Biol. Chem. 278: 32608-32617 [Abstract] [Full Text]  
  • Giese, K. C., Vierling, E. (2002). Changes in Oligomerization Are Essential for the Chaperone Activity of a Small Heat Shock Protein in Vivo and in Vitro. J. Biol. Chem. 277: 46310-46318 [Abstract] [Full Text]  
  • Kuczynska-Wisnik, D., Kcdzierska, S., Matuszewska, E., Lund, P., Taylor, A., Lipinska, B., Laskowska, E. (2002). The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock. Microbiology 148: 1757-1765 [Abstract] [Full Text]  
  • Narberhaus, F. (2002). {alpha}-Crystallin-Type Heat Shock Proteins: Socializing Minichaperones in the Context of a Multichaperone Network. Microbiol. Mol. Biol. Rev. 66: 64-93 [Abstract] [Full Text]  
  • Watanabe, Y.-h., Motohashi, K., Yoshida, M. (2002). Roles of the Two ATP Binding Sites of ClpB from Thermus thermophilus. J. Biol. Chem. 277: 5804-5809 [Abstract] [Full Text]  
  • Lesley, S. A., Graziano, J., Cho, C. Y., Knuth, M. W., Klock, H. E. (2002). Gene expression response to misfolded protein as a screen for soluble recombinant protein. Protein Eng Des Sel 15: 153-160 [Abstract] [Full Text]  
  • Ekaza, E., Teyssier, J., Ouahrani-Bettache, S., Liautard, J.-P., Köhler, S. (2001). Characterization of Brucella suis clpB and clpAB Mutants and Participation of the Genes in Stress Responses. J. Bacteriol. 183: 2677-2681 [Abstract] [Full Text]  
  • Ekaza, E., Guilloteau, L., Teyssier, J., Liautard, J.-P., Köhler, S. (2000). Functional analysis of the ClpATPase ClpA of Brucella suis, and persistence of a knockout mutant in BALB/c mice. Microbiology 146: 1605-1616 [Abstract] [Full Text]  
  • Zolkiewski, M. (1999). ClpB Cooperates with DnaK, DnaJ, and GrpE in Suppressing Protein Aggregation. A NOVEL MULTI-CHAPERONE SYSTEM FROM ESCHERICHIA COLI. J. Biol. Chem. 274: 28083-28086 [Abstract] [Full Text]  
  • Mason, C. A., Dünner, J., Indra, P., Colangelo, T. (1999). Heat-Induced Expression and Chemically Induced Expression of the Escherichia coli Stress Protein HtpG Are Affected by the Growth Environment. Appl. Environ. Microbiol. 65: 3433-3440 [Abstract] [Full Text]  
  • Motohashi, K., Watanabe, Y., Yohda, M., Yoshida, M. (1999). Heat-inactivated proteins are rescued by the DnaK·J-GrpE set and ClpB chaperones. Proc. Natl. Acad. Sci. USA 96: 7184-7189 [Abstract] [Full Text]  
  • Shearstone, J. R., Baneyx, F. (1999). Biochemical Characterization of the Small Heat Shock Protein IbpB from Escherichia coli. J. Biol. Chem. 274: 9937-9945 [Abstract] [Full Text]  
  • Studer, S., Narberhaus, F. (2000). Chaperone Activity and Homo- and Hetero-oligomer Formation of Bacterial Small Heat Shock Proteins. J. Biol. Chem. 275: 37212-37218 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»