Abstract
The min system prevents polar cell division in bacteria. Here, the biochemical characterization of the interaction of MinC and FtsZ from a Gram-positive bacterium, Bacillus subtilis, is reported. B. subtilis MinC inhibits FtsZ polymerization in a pH-dependent manner by preventing the formation of lateral associations between filaments. The inhibitory effect of MinC on FtsZ polymerization is counteracted by the presence of ZapA, a protein that promotes FtsZ filament bundling.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacillus subtilis / cytology*
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Bacillus subtilis / metabolism*
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Bacillus subtilis / ultrastructure
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Bacterial Proteins / antagonists & inhibitors*
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Bacterial Proteins / metabolism*
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Carrier Proteins / metabolism*
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Cell Division*
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Cytoskeletal Proteins / antagonists & inhibitors*
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Cytoskeletal Proteins / metabolism
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Hydrogen-Ion Concentration
Substances
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Bacterial Proteins
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Carrier Proteins
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Cytoskeletal Proteins
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FtsZ protein, Bacteria
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MinC protein, Bacteria