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- David Bramhill
- Department of Enzymology, Building 80Y-325, Merck Research Laboratories, P.O. Box 2000, Rahway, New Jersey 07065-0900;
抄録
<jats:p> ▪ Abstract Bacteria usually divide by building a central septum across the middle of the cell. This review focuses on recent results indicating that the tubulin-like FtsZ protein plays a central role in cytokinesis as a major component of a contractile cytoskeleton. Assembly of this cytoskeletal element abutting the membrane is a key point for regulation. The characterization of FtsZ homologues in Mycoplasmas, Archaea, and chloroplasts implies that the constriction mechanism is conserved and that FtsZ can constrict in the absence of peptidoglycan synthesis. In most Eubacteria, the internal cytoskeleton must also regulate synthesis of septal peptidoglycan. The Escherichia coli septum-specific penicillin-binding protein 3 (PBP3) forms a complex with other enzymes involved in murein metabolism, suggesting a centrally located transmembrane complex capable of splicing multiple new strands of peptidoglycan into the cell wall. Important questions remain about the spatial and temporal control of bacterial division. </jats:p>
収録刊行物
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- Annual Review of Cell and Developmental Biology
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Annual Review of Cell and Developmental Biology 13 (1), 395-424, 1997-11
Annual Reviews
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詳細情報 詳細情報について
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- CRID
- 1362825893396152576
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- NII論文ID
- 30022117583
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- ISSN
- 15308995
- 10810706
- http://id.crossref.org/issn/07434634
- http://id.crossref.org/issn/10810706
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