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

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Bisson-Filho, Alexandre W. ; Discola, Karen F. ; Castellen, Patricia ; Blasios, Valdir ; Martins, Alexandre ; Sforca, Mauricio L. ; Garcia, Wanius ; Zeri, Ana Carolina M. ; Erickson, Harold P. ; Dessen, Andrea ; Gueiros-Filho, Frederico J.

• Tipo de documento: Artigo Científico
• Fonte: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA; v. 112, n. 17, p. 9-pg., 2015-04-28.

Resumo

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. (AU)

• Processo FAPESP: 10/51866-0 - SMolBNet 2.0: combinando genética e RMN para dissecar interações proteína-proteína fundamentais para o funcionamento do complexo de divisão bacteriana
• Beneficiário: Frederico José Gueiros Filho
• Modalidade de apoio: Auxílio à Pesquisa - Regular