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

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Bisson-Filho, AW; Discola, KF; Castellen, P; Blasios, V; Martins, A; Sforça, ML; Garcia, W; Zeri, ACM; Erickson, HP; Dessen, A; Gueiros-Filho, FJ

Published Date

  • April 28, 2015

Published In

Volume / Issue

  • 112 / 17

Start / End Page

  • E2130 - E2138

PubMed ID

  • 25848052

Pubmed Central ID

  • PMC4418908

Electronic International Standard Serial Number (EISSN)

  • 1091-6490

Digital Object Identifier (DOI)

  • 10.1073/pnas.1414242112


  • eng

Conference Location

  • United States