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

Abstract : 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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Article dans une revue
Proceedings of the National Academy of Sciences of the United States of America , National Academy of Sciences, 2015, 112 (17), pp.E2130-8
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http://hal.univ-grenoble-alpes.fr/hal-01149454
Contributeur : Frank Thomas <>
Soumis le : jeudi 7 mai 2015 - 10:21:51
Dernière modification le : lundi 19 février 2018 - 14:34:03

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  • HAL Id : hal-01149454, version 1
  • PUBMED : 25848052

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Alexandre W Bisson-Filho, Karen F Discola, Patrícia Castellen, Valdir Blasios, Alexandre Martins, et al.. FtsZ filament capping by MciZ, a developmental regulator of bacterial division.. Proceedings of the National Academy of Sciences of the United States of America , National Academy of Sciences, 2015, 112 (17), pp.E2130-8. 〈hal-01149454〉

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