This Article
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 Nystrom, T.
Right arrow Articles by Neidhardt, F. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nystrom, T.
Right arrow Articles by Neidhardt, F. C.

 Previous Article  |  Next Article 

J. Bacteriol., 02 1996, 927-930, Vol 178, No. 3
Copyright © 1996, American Society for Microbiology

Effects of overproducing the universal stress protein, UspA, in Escherichia coli K-12

T Nystrom and FC Neidhardt
Department of General and Marine Microbiology, Lundberg Laboratory, University of Goteborg, Sweden.

A plasmid with the structural uspA gene under the control of a tac promoter was used to study the effects of altering uspA expression levels under various growth conditions. We found that increasing UspA synthesis to levels corresponding to physiologically induced levels decreased the cell growth rate in minimal medium and reduced or abolished the cells' capacity to adapt to upshift conditions. As was demonstrated by two-dimensional gel electrophoresis, increased uspA expression caused global changes in the pattern of protein synthesis. In addition, electrophoretic analysis together with V8 protease peptide mapping demonstrated that the pIs of some specific proteins became more acidic as a result of the elevation of the levels of UspA.


This article has been cited by other articles:

  • Wu, R., Wang, W., Yu, D., Zhang, W., Li, Y., Sun, Z., Wu, J., Meng, H., Zhang, H. (2009). Proteomics Analysis of Lactobacillus casei Zhang, a New Probiotic Bacterium Isolated from Traditional Home-made Koumiss in Inner Mongolia of China. Mol. Cell. Proteomics 8: 2321-2338 [Abstract] [Full Text]  
  • Hughes, V., Smith, S., Garcia-Sanchez, A., Sales, J., Stevenson, K. (2007). Proteomic comparison of Mycobacterium avium subspecies paratuberculosis grown in vitro and isolated from clinical cases of ovine paratuberculosis. Microbiology 153: 196-206 [Abstract] [Full Text]  
  • Nachin, L., Nannmark, U., Nystrom, T. (2005). Differential Roles of the Universal Stress Proteins of Escherichia coli in Oxidative Stress Resistance, Adhesion, and Motility. J. Bacteriol. 187: 6265-6272 [Abstract] [Full Text]  
  • Stubs, D., Fuchs, T. M., Schneider, B., Bosserhoff, A., Gross, R. (2005). Identification and regulation of cold-inducible factors of Bordetella bronchiseptica. Microbiology 151: 1895-1909 [Abstract] [Full Text]  
  • O'Toole, R., Smeulders, M. J., Blokpoel, M. C., Kay, E. J., Lougheed, K., Williams, H. D. (2003). A Two-Component Regulator of Universal Stress Protein Expression and Adaptation to Oxygen Starvation in Mycobacterium smegmatis. J. Bacteriol. 185: 1543-1554 [Abstract] [Full Text]  
  • Sauter, M., Rzewuski, G., Marwedel, T., Lorbiecke, R. (2002). The novel ethylene-regulated gene OsUsp1 from rice encodes a member of a plant protein family related to prokaryotic universal stress proteins. J Exp Bot 53: 2325-2331 [Abstract] [Full Text]  
  • Florczyk, M. A., McCue, L. A., Stack, R. F., Hauer, C. R., McDonough, K. A. (2001). Identification and Characterization of Mycobacterial Proteins Differentially Expressed under Standing and Shaking Culture Conditions, Including Rv2623 from a Novel Class of Putative ATP-Binding Proteins. Infect. Immun. 69: 5777-5785 [Abstract] [Full Text]  
  • Givskov, M., Östling, J., Eberl, L., Lindum, P. W., Christensen, A. B., Christiansen, G., Molin, S., Kjelleberg, S. (1998). Two Separate Regulatory Systems Participate in Control of Swarming Motility of Serratia liquefaciens MG1. J. Bacteriol. 180: 742-745 [Abstract] [Full Text]  
  • Aguilaniu, H., Gustafsson, L., Rigoulet, M., Nystrom, T. (2001). Protein Oxidation in G0 Cells of Saccharomyces cerevisiae Depends on the State Rather than Rate of Respiration and Is Enhanced in pos9 but Not yap1 Mutants. J. Biol. Chem. 276: 35396-35404 [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»