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 Fredriksson, A.
Right arrow Articles by Nyström, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fredriksson, A.
Right arrow Articles by Nyström, T.

 Previous Article  |  Next Article 

Journal of Bacteriology, June 2005, p. 4207-4213, Vol. 187, No. 12
0021-9193/05/$08.00+0     doi:10.1128/JB.187.12.4207-4213.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Defense against Protein Carbonylation by DnaK/DnaJ and Proteases of the Heat Shock Regulon

Åsa Fredriksson,1 Manuel Ballesteros,2 Sam Dukan,3 and Thomas Nyström1*

Department of Cell and Molecular Biology, Microbiology, Göteborg University, Box 462, 405 30 Göteborg, Sweden,1 Centro Andaluz de Biologia del Desarrollo (CABD), University "Pablo de Olavide," Ctra Utrera km1, ES-41013 Seville, Spain,2 Laboratoire de Chimie Bactérienne, CNRS-UPR9043, 31 Chemin Joseph Aiguier, 13402 Marseille, France3

Received 21 January 2005/ Accepted 8 March 2005

Protein carbonylation is an irreversible oxidative modification that increases during organism aging and bacterial growth arrest. We analyzed whether the heat shock regulon has a role in defending Escherichia coli cells against this deleterious modification upon entry into stationary phase. Providing the cell with ectopically elevated levels of the heat shock transcription factor, {sigma}32, effectively reduced stasis-induced carbonylation. Separate overproduction of the major chaperone systems, DnaK/DnaJ and GroEL/GroES, established that the former of these is more important in counteracting protein carbonylation. Deletion of the heat shock proteases Lon and HslVU enhanced carbonylation whereas a clpP deletion alone had no effect. However, ClpP appears to have a role in reducing protein carbonyls in cells lacking Lon and HslVU. Proteomic immunodetection of carbonylated proteins in the wild-type, lon, and hslVU strains demonstrated that the same spectrum of proteins displayed a higher load of carbonyl groups in the lon and hslVU mutants. These proteins included the ß-subunit of RNA polymerase, elongation factors Tu and G, the E1 subunit of the pyruvate dehydrogenase complex, isocitrate dehydrogenase, 6-phosphogluconate dehydrogenase, and serine hydroxymethyltranferase.

* Corresponding author. Mailing address: Department of Cell and Molecular Biology, Microbiology, Medicinaregatan 9C, 413 90 Göteborg, Sweden. Phone: 46 31 7732582. Fax: 46 31 7732599. E-mail: thomas.nystrom{at}gmm.gu.se.

Journal of Bacteriology, June 2005, p. 4207-4213, Vol. 187, No. 12
0021-9193/05/$08.00+0     doi:10.1128/JB.187.12.4207-4213.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Wright, J. A., Grant, A. J., Hurd, D., Harrison, M., Guccione, E. J., Kelly, D. J., Maskell, D. J. (2009). Metabolite and transcriptome analysis of Campylobacter jejuni in vitro growth reveals a stationary-phase physiological switch. Microbiology 155: 80-94 [Abstract] [Full Text]  
  • Maisonneuve, E., Fraysse, L., Lignon, S., Capron, L., Dukan, S. (2008). Carbonylated Proteins Are Detectable Only in a Degradation-Resistant Aggregate State in Escherichia coli. J. Bacteriol. 190: 6609-6614 [Abstract] [Full Text]  
  • Matuszewska, E., Kwiatkowska, J., Kuczynska-Wisnik, D., Laskowska, E. (2008). Escherichia coli heat-shock proteins IbpA/B are involved in resistance to oxidative stress induced by copper. Microbiology 154: 1739-1747 [Abstract] [Full Text]  
  • Kizer, L., Pitera, D. J., Pfleger, B. F., Keasling, J. D. (2008). Application of Functional Genomics to Pathway Optimization for Increased Isoprenoid Production. Appl. Environ. Microbiol. 74: 3229-3241 [Abstract] [Full Text]  
  • Erjavec, N., Larsson, L., Grantham, J., Nystrom, T. (2007). Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p. Genes Dev. 21: 2410-2421 [Abstract] [Full Text]  
  • Manes, N. P., Gustin, J. K., Rue, J., Mottaz, H. M., Purvine, S. O., Norbeck, A. D., Monroe, M. E., Zimmer, J. S. D., Metz, T. O., Adkins, J. N., Smith, R. D., Heffron, F. (2007). Targeted Protein Degradation by Salmonella under Phagosome-mimicking Culture Conditions Investigated Using Comparative Peptidomics. Mol. Cell. Proteomics 6: 717-727 [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»