期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 112, 期 17, 页码 E2130-E2138出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1414242112
关键词
FtsZ; cell division; cytokinesis; filament capping; bacterial cytoskeleton
资金
- French Infrastructure for Structural Biology [ANR-10-NSB-05-02]
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [10/51866-0]
- Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES) [1169/2013]
- National Institute of Health [GM66014]
- FAPESP from Science without Borders program
- FAPESP
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [10/51866-0] Funding Source: FAPESP
Cytoskeletal structures are dynamically remodeled with the aid of regulatory proteins. FtsZ (filamentation temperature-sensitive Z) is the bacterial homolog of tubulin that polymerizes into rings localized to cell-division sites, and the constriction of these rings drives cytokinesis. Here we investigate the mechanism by which the Bacillus subtilis cell-division inhibitor, MciZ (mother cell inhibitor of FtsZ), blocks assembly of FtsZ. The X-ray crystal structure reveals that MciZ binds to the C-terminal polymerization interface of FtsZ, the equivalent of the minus end of tubulin. Using in vivo and in vitro assays and microscopy, we show that MciZ, at substoichiometric levels to FtsZ, causes shortening of protofilaments and blocks the assembly of higher-order FtsZ structures. The findings demonstrate an unanticipated capping-based regulatory mechanism for FtsZ.
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