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- Article] A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ
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DocNo of ILP: 6156
Doc. Type: Article
Title: A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ
Authors: Gueiros, FJ; Losick, R
Full Name of Authors: Gueiros, FJ; Losick, R
Keywords by Author: FtsZ; cytokinesis; Bacillus subtilis; protein localization
Keywords Plus: ESCHERICHIA-COLI-CELLS; TO-POLE OSCILLATION; BACILLUS-SUBTILIS; GTP HYDROLYSIS; RING FORMATION; MICROTUBULE DYNAMICS; MINICELL LOCUS; INHIBITOR MINC; RAPID POLE; SITE
Abstract: Cell division in bacteria is mediated by the tubulin-like protein FtsZ, which assembles into a structure known as the Z ring at the future site of cytokinesis. We report the discovery of a Z-ring-associated protein in Bacillus subtilis called ZapA. ZapA was found to colocalize with the Z ring in vivo and was capable of binding to FtsZ and stimulating the formation of higher-order assemblies of the cytokinetic protein in vitro. The absence of ZapA alone did not impair cell viability, but the absence of ZapA in combination with the absence of a second, dispensable division protein EzrA caused a severe block in cytokinesis. The absence of ZapA also caused lethality in cells producing lower than normal levels of FtsZ or lacking the division-site-selection protein DivIVA. Conversely, overproduction of ZapA reversed the toxicity of excess levels of the division inhibitor MinD). In toto, the evidence indicates that ZapA is part of the cytokinetic machinery of the cell and acts by promoting Z-ring formation. Finally, ZapA is widely conserved among bacteria with apparent orthologs in many species, including Escherichia coli, in which the orthologous protein exhibited a strikingly similar pattern of subcellular localization to that of ZapA. Members of the ZapA family of proteins are likely to be a common feature of the cytokinetic machinery in bacteria.
Cate of OECD: Biological sciences
Year of Publication: 2002
Business Area: other
Detail Business: medicine & science
Country: USA
Study Area:
Name of Journal: GENES & DEVELOPMENT
Language: English
Country of Authors: Harvard Univ, Dept Mol & Cellular Biol, Cambridge, MA 02138 USA
Press Adress: Losick, R (reprint author), Harvard Univ, Dept Mol & Cellular Biol, Cambridge, MA 02138 USA.
Email Address:
Citaion:
Funding:
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Number of Citaion: 60
Publication: COLD SPRING HARBOR LAB PRESS
City of Publication: PLAINVIEW
Address of Publication: 1 BUNGTOWN RD, PLAINVIEW, NY 11724 USA
ISSN: 0890-9369
29-Character Source Abbreviation: GENE DEV
ISO Source Abbreviation: Genes Dev.
Volume: 16
Version: 19
Start of File: 2544
End of File: 2556
DOI: 10.1101/gad.1014102
Number of Pages: 13
Web of Science Category: Cell Biology; Developmental Biology; Genetics & Heredity
Subject Category: Cell Biology; Developmental Biology; Genetics & Heredity
Document Delivery Number: 601UZ
Unique Article Identifier: WOS:000178468000010
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