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Journal of Bacteriology, January 2009, p. 333-346, Vol. 191, No. 1
0021-9193/09/$08.00+0     doi:10.1128/JB.00331-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Characterization of YmgF, a 72-Residue Inner Membrane Protein That Associates with the Escherichia coli Cell Division Machinery{triangledown} ,{dagger}

Gouzel Karimova, Carine Robichon, and Daniel Ladant*

Institut Pasteur, CNRS URA 2185, Unité de Biochimie des Interactions Macromoléculaires, Département de Biologie Structurale et Chimie, 25 rue du Dr Roux, Paris Cedex 15, France

Received 5 March 2008/ Accepted 24 October 2008

Formation of the Escherichia coli division septum is catalyzed by a number of essential proteins (named Fts) that assemble into a ring-like structure at the future division site. Many of these Fts proteins are intrinsic transmembrane proteins whose functions are largely unknown. In the present study, we attempted to identify a novel putative component(s) of the E. coli cell division machinery by searching for proteins that could interact with known Fts proteins. To do that, we used a bacterial two-hybrid system based on interaction-mediated reconstitution of a cyclic AMP (cAMP) signaling cascade to perform a library screening in order to find putative partners of E. coli cell division protein FtsL. Here we report the characterization of YmgF, a 72-residue integral membrane protein of unknown function that was found to associate with many E. coli cell division proteins and to localize to the E. coli division septum in an FtsZ-, FtsA-, FtsQ-, and FtsN-dependent manner. Although YmgF was previously shown to be not essential for cell viability, we found that when overexpressed, YmgF was able to overcome the thermosensitive phenotype of the ftsQ1(Ts) mutation and restore its viability under low-osmolarity conditions. Our results suggest that YmgF might be a novel component of the E. coli cell division machinery.

* Corresponding author. Mailing address: Department of Structural Biology and Chemistry, Institut Pasteur, 28 rue du Docteur Roux, Paris 75015, France. Phone: 33145688400. Fax: 33140613042. E-mail: ladant{at}pasteur.fr

{triangledown} Published ahead of print on 31 October 2008.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

Journal of Bacteriology, January 2009, p. 333-346, Vol. 191, No. 1
0021-9193/09/$08.00+0     doi:10.1128/JB.00331-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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  • Arends, S. J. R., Kustusch, R. J., Weiss, D. S. (2009). ATP-Binding Site Lesions in FtsE Impair Cell Division. J. Bacteriol. 191: 3772-3784 [Abstract] [Full Text]  


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