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Vol. 16, No. 19, pp. 2544-2556, October 1, 2002
Department of Molecular and Cellular Biology, Harvard University,
Cambridge Massachusetts 02138, USA
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.
[Key Words: FtsZ; cytokinesis; Bacillus subtilis; protein localization]
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