FtsZ filament capping by MciZ, a developmental regulator of bacterial division.
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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.
Cell Cycle Proteins
Protein Structure, Quaternary
Protein Structure, Tertiary
Published Version (Please cite this version)10.1073/pnas.1414242112
Publication InfoBisson-Filho, Alexandre W; Blasios, Valdir; Castellen, Patrícia; Dessen, Andréa; Discola, Karen F; Erickson, Harold Paul; ... Zeri, Ana Carolina M (2015). FtsZ filament capping by MciZ, a developmental regulator of bacterial division. Proceedings of the National Academy of Sciences of the United States of America, 112(17). 10.1073/pnas.1414242112. Retrieved from https://hdl.handle.net/10161/16451.
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James B. Duke Professor of Cell Biology
Cytoskeleton: It is now clear that the actin and microtubule cytoskeleton originated in bacteria. Our major research is on FtsZ, the bacterial tubulin homolog, which assembles into a contractile ring that divides the bacterium. We have studied FtsZ assembly in vitro, and found that it assembles into thin protofilaments (pfs). Dozens of these pfs are further clustered to form the contractile Z-ring in vivo. Some important discoveries in the last ten years include: &bul
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