Electronic Resource
Palo Alto, Calif.
:
Annual Reviews
Annual Review of Genetics
33 (1999), S. 423-448
ISSN:
0066-4197
Source:
Annual Reviews Electronic Back Volume Collection 1932-2001ff
Topics:
Biology
Notes:
Abstract Formation of the bacterial division septum is catalyzed by a number of essential proteins that assemble into a ring structure at the future division site. Assembly of proteins into the cytokinetic ring appears to occur in a hierarchial order that is initiated by the FtsZ protein, a structural and functional analog of eukaryotic tubulins. Placement of the division site at its correct location in Escherichia coli requires a division inhibitor (MinC), that is responsible for preventing septation at unwanted sites near the cell poles, and a topological specificity protein (MinE), that forms a ring at midcell and protects the midcell site from the division inhibitor. However, the mechanism responsible for identifying the position of the midcell site or the polar sites used for spore septum formation is still unclear. Regulation of the division process and its coordination with other cell cycle events, such as chromosome replication, are poorly understood. However, a protein has been identified in Caulobacter (CtrA) that regulates both the initiation of chromosome regulation and the transcription of ftsZ, and that may play an important role in the coordination process.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1146/annurev.genet.33.1.423
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