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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
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Bisson-Filho, Alexandre W. [1] ; Discola, Karen F. [2, 3, 4] ; Castellen, Patricia [1, 5] ; Blasios, Valdir [1] ; Martins, Alexandre [2, 3, 4] ; Sforca, Mauricio L. [5] ; Garcia, Wanius [6] ; Zeri, Ana Carolina M. [5] ; Erickson, Harold P. [7] ; Dessen, Andrea [2, 3, 4, 5] ; Gueiros-Filho, Frederico J. [1]
Total Authors: 11
Affiliation:
[1] Univ Sao Paulo, IQ, Dept Bioquim, BR-05508000 Sao Paulo, SP - Brazil
[2] Univ Grenoble Alpes, F-38044 Grenoble - France
[3] CNRS, F-38044 Grenoble - France
[4] Commissariat Energie Atom & Energies Alternat, Inst Biol Struct, F-38044 Grenoble - France
[5] CNPEM, Brazilian Biosci Natl Lab, LNBio, BR-13083970 Campinas, SP - Brazil
[6] Univ Fed ABC, Ctr Ciencias Nat & Humanas, BR-09210580 Santo Andre, SP - Brazil
[7] Duke Univ, Med Ctr, Dept Cell Biol, Durham, NC 27710 - USA
Total Affiliations: 7
Document type: Journal article
Source: Proceedings of the National Academy of Sciences of the United States of America; v. 112, n. 17, p. E2130-E2138, APR 28 2015.
Web of Science Citations: 24
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. (AU)

FAPESP's process: 10/51866-0 - SMolBNet 2.0: combining genetics and NMR to dissect fundamental protein-protein interactions for complex bacterial division
Grantee:Frederico José Gueiros Filho
Support type: Regular Research Grants