Redefining the roles of the FtsZ-ring in bacterial cytokinesis.
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.
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. Electronic address: xiao@jhmi.edu.
Jie
J
Xiao
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. Electronic address: egoley1@jhmi.edu.
Erin D
ED
Goley
D001419:Bacteria / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D002473:Cell Wall / Q000378:metabolism; D048749:Cytokinesis; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000502:physiology; D010457:Peptidoglycan / Q000378:metabolism
D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria; D010457:Peptidoglycan