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- W2124514849 endingPage "154" @default.
- W2124514849 startingPage "125" @default.
- W2124514849 abstract "FtsZ is a prokaryotic tubulin homolog that assembles into a ring at the future site of cell division. The resulting Z ring forms the framework for the division apparatus, and its assembly is regulated throughout the bacterial cell cycle. A highly dynamic structure, the Z ring exhibits continual subunit turnover and the ability to rapidly assemble, disassemble, and, under certain circumstances, relocalize. These in vivo properties are ultimately due to FtsZ's capacity for guanosine triphosphate (GTP)-dependent, reversible polymerization. FtsZ polymer stability appears to be fine-tuned such that subtle changes in its assembly kinetics result in large changes in the Z ring structure. Thus, regulatory proteins that modulate FtsZ's assembly dynamics can cause the ring to rapidly remodel in response to developmental and environmental cues." @default.
- W2124514849 created "2016-06-24" @default.
- W2124514849 creator A5034275737 @default.
- W2124514849 creator A5085076715 @default.
- W2124514849 date "2003-10-01" @default.
- W2124514849 modified "2023-09-25" @default.
- W2124514849 title "Assembly Dynamics of the Bacterial Cell Division Protein FtsZ: Poised at the Edge of Stability" @default.
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