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EzrA Prevents Aberrant Cell Division by Modulating Assembly of the Cytoskeletal Protein FtsZ

Overview
Journal Mol Microbiol
Date 2004 Apr 23
PMID 15101985
Citations 59
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Abstract

In response to a cell cycle signal, the cytoskeletal protein FtsZ assembles into a ring structure that establishes the location of the division site and serves as a framework for assembly of the division machinery. A battery of factors control FtsZ assembly to ensure that the ring forms in the correct position and at the precise time. EzrA, a negative regulator of FtsZ ring formation, is important for ensuring that the ring forms only once per cell cycle and that cytokinesis is restricted to mid-cell. EzrA is distributed throughout the plasma membrane and localizes to the ring in an FtsZ-dependent manner, suggesting that it interacts directly with FtsZ to modulate assembly. We have performed a series of experiments examining the interaction between EzrA and FtsZ. As little as twofold overexpression of EzrA blocks FtsZ ring formation in a sensitized genetic background, consistent with its predicted function. A purified EzrA fusion protein interacts directly with FtsZ to block assembly in vitro. Although EzrA is able to inhibit FtsZ assembly, it is unable to disassemble preformed polymers. These data support a model in which EzrA interacts directly with FtsZ at the plasma membrane to prevent polymerization and aberrant FtsZ ring formation.

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References
1.
Daniel R, Harry E, Katis V, Wake R, Errington J . Characterization of the essential cell division gene ftsL(yIID) of Bacillus subtilis and its role in the assembly of the division apparatus. Mol Microbiol. 1998; 29(2):593-604. DOI: 10.1046/j.1365-2958.1998.00954.x. View

2.
Levin P, Kurtser I, Grossman A . Identification and characterization of a negative regulator of FtsZ ring formation in Bacillus subtilis. Proc Natl Acad Sci U S A. 1999; 96(17):9642-7. PMC: 22263. DOI: 10.1073/pnas.96.17.9642. View

3.
Quisel J, Burkholder W, Grossman A . In vivo effects of sporulation kinases on mutant Spo0A proteins in Bacillus subtilis. J Bacteriol. 2001; 183(22):6573-8. PMC: 95488. DOI: 10.1128/JB.183.22.6573-6578.2001. View

4.
Gelb M . Protein prenylation, et cetera: signal transduction in two dimensions. Science. 1997; 275(5307):1750-1. DOI: 10.1126/science.275.5307.1750. View

5.
Cordell S, Robinson E, Lowe J . Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ. Proc Natl Acad Sci U S A. 2003; 100(13):7889-94. PMC: 164683. DOI: 10.1073/pnas.1330742100. View