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PublicationTrends in Microbiology
Year2010
Volume18
Pages348 – 356
International

Strong FtsZ is with the force: mechanisms to constrict bacteria

Authors:Jesus Mingorance , German Rivas , Marisela Vélez Tirado, Paulino Gomez-Puertas , Miguel Vicente
Groups of research:Biofunctional surfaces laboratory
FtsZ, the best-known prokaryotic division protein, assembles at midcell with other proteins forming a ring during septation. Widely conserved in bacteria, FtsZ represents the ancestor of tubulin. In the presence of GTP it forms polymers able to associate into multistranded flexible structures. FtsZ research is aimed at determining the role of the Z-ring in division, describing the polymerization and potential force-generating mechanisms and evaluating the roles of nucleotide exchange and hydrolysis. Systems to reconstruct the FtsZ ring in vitro have been described and some of its mechanical properties have been reproduced using in silico modeling. We discuss current research in FtsZ, some of the controversies, and finally propose further research needed to complete a model of FtsZ action that reconciles its in vitro properties with its role in division.
Keywords:bacterial cell division, review
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