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YeeV is an Escherichia Coli Toxin That Inhibits Cell Division by Targeting the Cytoskeleton Proteins, FtsZ and MreB

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Journal Mol Microbiol
Date 2010 Dec 21
PMID 21166897
Citations 76
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Abstract

Toxin-antitoxin (TA) systems of free-living bacteria have recently demonstrated that these toxins inhibit cell growth by targeting essential functions of cellular metabolism. Here we show that YeeV toxin inhibits cell division, leads to a change in morphology and lysis of Escherichia coli cells. YeeV interacts with two essential cytoskeleton proteins, FtsZ and MreB. Purified YeeV inhibits both the GTPase activity and the GTP-dependent polymerization of FtsZ. YeeV also inhibits ATP-dependent polymerization of MreB. Truncated C-terminal deletions of YeeV result in elongation of cells, and a deletion of the first 15 amino acids from the N-terminus of YeeV caused lemon-shaped cell formation. The YeeV toxin is distinct from other well-studied toxins: it directs the binding of two cytoskeletal proteins and inhibits FtsZ and MreB simultaneously.

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References
1.
Dajkovic A, Lan G, Sun S, Wirtz D, Lutkenhaus J . MinC spatially controls bacterial cytokinesis by antagonizing the scaffolding function of FtsZ. Curr Biol. 2008; 18(4):235-44. DOI: 10.1016/j.cub.2008.01.042. View

2.
Mukherjee A, Cao C, Lutkenhaus J . Inhibition of FtsZ polymerization by SulA, an inhibitor of septation in Escherichia coli. Proc Natl Acad Sci U S A. 1998; 95(6):2885-90. PMC: 19664. DOI: 10.1073/pnas.95.6.2885. View

3.
Wachi M, Matsuhashi M . Negative control of cell division by mreB, a gene that functions in determining the rod shape of Escherichia coli cells. J Bacteriol. 1989; 171(6):3123-7. PMC: 210024. DOI: 10.1128/jb.171.6.3123-3127.1989. View

4.
Hurley J, Woychik N . Bacterial toxin HigB associates with ribosomes and mediates translation-dependent mRNA cleavage at A-rich sites. J Biol Chem. 2009; 284(28):18605-13. PMC: 2707191. DOI: 10.1074/jbc.M109.008763. View

5.
Varma A, de Pedro M, Young K . FtsZ directs a second mode of peptidoglycan synthesis in Escherichia coli. J Bacteriol. 2007; 189(15):5692-704. PMC: 1951832. DOI: 10.1128/JB.00455-07. View