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Curr Opin Microbiol. 2016 Dec;34:90-96. doi: 10.1016/j.mib.2016.08.008. Epub 2016 Sep 10.

Redefining the roles of the FtsZ-ring in bacterial cytokinesis.

Author information

1
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. Electronic address: xiao@jhmi.edu.
2
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. Electronic address: egoley1@jhmi.edu.

Abstract

In most bacteria, cell division relies on the functions of an essential protein, FtsZ. FtsZ polymerizes at the future division site to form a ring-like structure, termed the Z-ring, that serves as a scaffold to recruit all other division proteins, and possibly generates force to constrict the cell. The scaffolding function of the Z-ring is well established, but the force generating function has recently been called into question. Additionally, new findings have demonstrated that the Z-ring is more directly linked to cell wall metabolism than simply recruiting enzymes to the division site. Here we review these advances and suggest that rather than generating a rate-limiting constrictive force, the Z-ring's function may be redefined as an orchestrator of septum synthesis.

PMID:
27620716
PMCID:
PMC5164845
DOI:
10.1016/j.mib.2016.08.008
[Indexed for MEDLINE]
Free PMC Article

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