期刊
TRENDS IN MICROBIOLOGY
卷 18, 期 8, 页码 348-356出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.tim.2010.06.001
关键词
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资金
- Comunidad de Madrid [COMBACT S-BIO-0260/2006-]
- European Commision [HEALTH-F3-2009-223431]
- Ministerio de Ciencia e Innovacion, Spain [BIO2008-04478-C03-00]
- Ministerio de Ciencia e Innovacion [CSD2007-00010]
- Biomol-Informatics S.L.
- European Social Fund
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 multi-stranded 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 silica 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.
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