Journal
SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY
Volume 37, Issue -, Pages 3-10Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.semcdb.2014.09.017
Keywords
FtsZ; Cell division; Cytokinetic ring; Cooperative assembly; Intrinsically disordered peptide; Bacteria
Categories
Funding
- National Institutes of Health Public Health Service [GM64671]
- National Science Foundation [MCB-1121867]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1121867] Funding Source: National Science Foundation
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In bacteria, animals, fungi, and many single celled eukaryotes, division is initiated by the formation of a ring of cytoskeletal protein at the nascent division site. In bacteria, the tubulin-like GTPase FtsZ serves as the foundation for the cytokinetic ring. A conserved feature of FtsZ is an intrinsically disordered peptide known as the C-terminal linker. Chimeric experiments suggest the linker acts as a flexible boom allowing FtsZ to associate with the membrane through a conserved C-terminal domain and also modulates interactions both between FtsZ subunits and between FtsZ and modulatory proteins in the cytoplasm. (C) 2014 Elsevier Ltd. All rights reserved.
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