期刊
BIOPHYSICAL JOURNAL
卷 95, 期 8, 页码 4045-4056出版社
CELL PRESS
DOI: 10.1529/biophysj.108.132837
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资金
- National Institutes of Health [GM075305]
- National Science Foundation [CHE-0547041]
- Institute for NanoBioTechnology at The Johns Hopkins University
FtsZ is a tubulin homolog essential for prokaryotic cell division. In living bacteria, FtsZ forms a ringlike structure (Z-ring) at the cell midpoint. Cell division coincides with a gradual contraction of the Z-ring, although the detailed molecular structure of the Z-ring is unknown. To reveal the structural properties of FtsZ, an understanding of FtsZ. lament and bundle formation is needed. We develop a kinetic model that describes the polymerization and bundling mechanism of FtsZ. laments. The model reveals the energetics of the FtsZ. lament formation and the bundling energy between. laments. A weak lateral interaction between. laments is predicted by the model. The model is able to fit the in vitro polymerization kinetics data of another researcher, and explains the cooperativity observed in FtsZ kinetics and the critical concentration in different buffer media. The developed model is also applicable for understanding the kinetics and energetics of other bundling biopolymer. laments.
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