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 Gutiérrez, P.
Right arrow Articles by Gehring, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gutiérrez, P.
Right arrow Articles by Gehring, K.

 Previous Article  |  Next Article 

Journal of Bacteriology, May 2005, p. 3496-3501, Vol. 187, No. 10
0021-9193/05/$08.00+0     doi:10.1128/JB.187.10.3496-3501.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Solution Structure of the Carbon Storage Regulator Protein CsrA from Escherichia coli

Pablo Gutiérrez, Yan Li, Michael J. Osborne, Ekaterina Pomerantseva, Qian Liu, and Kalle Gehring*

Department of Biochemistry, McGill University, 3655 Promenade Sir William Osler, Montreal, Quebec, Canada H3G 1Y6

Received 14 November 2004/ Accepted 11 February 2005

The carbon storage regulator A (CsrA) is a protein responsible for the repression of a variety of stationary-phase genes in bacteria. In this work, we describe the nuclear magnetic resonance (NMR)-based structure of the CsrA dimer and its RNA-binding properties. CsrA is a dimer of two identical subunits, each composed of five strands, a small {alpha}-helix and a flexible C terminus. NMR titration experiments suggest that the ß1-ß2 and ß3-ß4 loops and the C-terminal helix are important elements in RNA binding. Even though the ß3-ß4 loop contains a highly conserved RNA-binding motif, GxxG, typical of KH domains, our structure excludes CsrA from being a member of this protein family, as previously suggested. A mechanism for the recognition of mRNAs downregulated by CsrA is proposed.

* Corresponding author. Mailing address: Department of Biochemistry, McGill University, 3655 Promenade Sir William Osler, Montreal, Quebec, Canada H3G 1Y6. Phone: (514) 398-7287. Fax: (514) 398-7384. E-mail: kalle.gehring{at}mcgill.ca.

Journal of Bacteriology, May 2005, p. 3496-3501, Vol. 187, No. 10
0021-9193/05/$08.00+0     doi:10.1128/JB.187.10.3496-3501.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Bhatt, S., Edwards, A. N., Nguyen, H. T. T., Merlin, D., Romeo, T., Kalman, D. (2009). The RNA Binding Protein CsrA Is a Pleiotropic Regulator of the Locus of Enterocyte Effacement Pathogenicity Island of Enteropathogenic Escherichia coli. Infect. Immun. 77: 3552-3568 [Abstract] [Full Text]  
  • Lucchetti-Miganeh, C., Burrowes, E., Baysse, C., Ermel, G. (2008). The post-transcriptional regulator CsrA plays a central role in the adaptation of bacterial pathogens to different stages of infection in animal hosts. Microbiology 154: 16-29 [Abstract] [Full Text]  
  • Mercante, J., Suzuki, K., Cheng, X., Babitzke, P., Romeo, T. (2006). Comprehensive Alanine-scanning Mutagenesis of Escherichia coli CsrA Defines Two Subdomains of Critical Functional Importance. J. Biol. Chem. 281: 31832-31842 [Abstract] [Full Text]  
  • Galperin, M. Y. (2006). Structural classification of bacterial response regulators: diversity of output domains and domain combinations.. J. Bacteriol. 188: 4169-4182 [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»