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Biochem Biophys Res Commun. 1995 Apr 6;209(1):198-204.

A cell division inhibitor SulA of Escherichia coli directly interacts with FtsZ through GTP hydrolysis.

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  • 1Department of Microbial Genetics, National Institute of Genetics, Mishima, Japan.


E. coli SulA is an SOS-inducible protein that inhibits cell division. FtsZ is a protein that plays a central role in bacterial cell division. Using purified SulA protein that was fused to the maltose binding protein, we demonstrate in vitro that SulA interacts with FtsZ to form a stable complex. The reaction requires GTP and Mg ion. GDP and GTP gamma S cannot substitute for GTP, which suggests that hydrolysis of GTP is required for the reaction. The complex is formed in a molar ratio of approximately one to one of the two proteins. It is likely that the complex formation represents the in vivo mechanism by which SulA inhibits cell division.

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