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Journal of Bacteriology, April 2005, p. 2233-2243, Vol. 187, No. 7
0021-9193/05/$08.00+0     doi:10.1128/JB.187.7.2233-2243.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Interaction Network among Escherichia coli Membrane Proteins Involved in Cell Division as Revealed by Bacterial Two-Hybrid Analysis

Gouzel Karimova,1* Nathalie Dautin,1,{dagger} and Daniel Ladant1

Unité de Biochimie des Interactions Macromoléculaires, Département de Biologie Structurale et Chimie, CNRS URA 2185, Institut Pasteur, Paris, France1

Received 30 July 2004/ Accepted 3 January 2005

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. Several of these Fts proteins are intrinsic transmembrane proteins whose functions are largely unknown. Although these proteins appear to be recruited to the division site in a hierarchical order, the molecular interactions underlying the assembly of the cell division machinery remain mostly unspecified. In the present study, we used a bacterial two-hybrid system based on interaction-mediated reconstitution of a cyclic AMP (cAMP) signaling cascade to unravel the molecular basis of septum assembly by analyzing the protein interaction network among E. coli cell division proteins. Our results indicate that the Fts proteins are connected to one another through multiple interactions. A deletion mapping analysis carried out with two of these proteins, FtsQ and FtsI, revealed that different regions of the polypeptides are involved in their associations with their partners. Furthermore, we showed that the association between two Fts hybrid proteins could be modulated by the coexpression of a third Fts partner. Altogether, these data suggest that the cell division machinery assembly is driven by the cooperative association among the different Fts proteins to form a dynamic multiprotein structure at the septum site. In addition, our study shows that the cAMP-based two-hybrid system is particularly appropriate for analyzing molecular interactions between membrane proteins.

* Corresponding author. Mailing address: Unité de Biochimie des Interactions Macromoléculaires, Institut Pasteur, 75724 Paris, Cedex 15, France. Phone: (33) 145688388. Fax: (33) 140613043. E-mail: karimova{at}pasteur.fr.

{dagger} Present address: Genetics and Biochemistry Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-1810.

Journal of Bacteriology, April 2005, p. 2233-2243, Vol. 187, No. 7
0021-9193/05/$08.00+0     doi:10.1128/JB.187.7.2233-2243.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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