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
Google Scholar
Right arrow Articles by Simm, R.
Right arrow Articles by Römling, U.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Simm, R.
Right arrow Articles by Römling, U.

 Previous Article  |  Next Article 

Journal of Bacteriology, June 2009, p. 3928-3937, Vol. 191, No. 12
0021-9193/09/$08.00+0     doi:10.1128/JB.00290-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

A Role for the EAL-Like Protein STM1344 in Regulation of CsgD Expression and Motility in Salmonella enterica Serovar Typhimurium{triangledown}

Roger Simm,{dagger} Uwe Remminghorst, Irfan Ahmad, Katherina Zakikhany, and Ute Römling*

Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Stockholm, Sweden

Received 4 March 2009/ Accepted 8 April 2009

The bacterial second messenger cyclic di-GMP (c-di-GMP) regulates the transition between sessility and motility. In Salmonella enterica serovar Typhimurium, the expression of CsgD, the regulator of multicellular rdar morphotype behavior, is a major target of c-di-GMP signaling. CsgD expression is positively regulated by at least two diguanylate cyclases, GGDEF domain proteins, and negatively regulated by at least four phosphodiesterases, EAL domain proteins. Here, we show that in contrast to EAL domain proteins acting as phosphodiesterases, the EAL-like protein STM1344 regulated CsgD expression positively and motility negatively. STM1344, however, did not have a role in c-di-GMP turnover and also did not bind the nucleotide. STM1344 acted upstream of the phosphodiesterases STM1703 and STM3611, previously identified to participate in CsgD downregulation, where it repressed their expression. Consequently, although STM1344 has not retained a direct role in c-di-GMP metabolism, it still participates in the regulation of c-di-GMP turnover and has a role in the transition between sessility and motility.

* Corresponding author. Mailing address: Dept. of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Nobels väg 16, Stockholm, Sweden. Phone: 46-8-52487319. Fax: 46-8-311101. E-mail: ute.romling{at}ki.se

{triangledown} Published ahead of print on 17 April 2009.

{dagger} Present address: Laboratory for Microbial Dynamics, Department of Pharmaceutical Biosciences, University of Oslo, Oslo, Norway.

Journal of Bacteriology, June 2009, p. 3928-3937, Vol. 191, No. 12
0021-9193/09/$08.00+0     doi:10.1128/JB.00290-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Romling, U. (2009). Rationalizing the Evolution of EAL Domain-Based Cyclic di-GMP-Specific Phosphodiesterases. J. Bacteriol. 191: 4697-4700 [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»