FtsZ filament capping by MciZ, a developmental regulator of bacterial division.


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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Publication Info

Bisson-Filho, Alexandre W, Karen F Discola, Patrícia Castellen, Valdir Blasios, Alexandre Martins, Maurício L Sforça, Wanius Garcia, Ana Carolina M Zeri, et al. (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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Harold Paul Erickson

James B. Duke Distinguished Professor Emeritus

Recent research has been on cytoskeleton (eukaryotes and bacteria); a skirmish to debunk the irisin story; a reinterpretation of proposed multivalent binders of the coronavirus spike protein. I have also published an ebook on "Principles of Protein-Protein Association" suitable for a course module or individual learning.

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