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• W2045134865 startingPage "1407" @default.
• W2045134865 abstract "ZipA is an essential component of the cell division machinery in E. coli and other closely related bacteria. It is an integral membrane protein that binds to FtsZ, tethering it to the inner membrane. ZipA also induces bundling of FtsZ protofilaments and may play a role in regulating FtsA activity; however, the molecular details behind these observations are not clear. In this study we have analyzed the oligomeric state of ZipA in vivo, by chemical cross-linking, and in vitro, by native gel electrophoresis (BN-PAGE). Our data indicate that ZipA can self-associate as a homodimer and that this self-interaction is not dependent on the FtsZ-binding domain. This observation rules out the possibility that FtsZ polymers mediate the ZipA self-interaction. Given this observation, it is possible that a certain population of ZipA is recruited to the division septum in a homodimeric form." @default.
• W2045134865 created "2016-06-24" @default.
• W2045134865 creator A5021432805 @default.
• W2045134865 creator A5072454967 @default.
• W2045134865 date "2012-02-09" @default.
• W2045134865 modified "2023-09-23" @default.
• W2045134865 title "The <i>Escherichia coli</i> Cell Division Protein ZipA Forms Homodimers Prior to Association with FtsZ" @default.
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• W2045134865 doi "https://doi.org/10.1021/bi2015647" @default.
• W2045134865 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22304478" @default.
• W2045134865 hasPublicationYear "2012" @default.
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