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The Escherichia coli Cell Division Protein ZipA Forms Homodimers Prior to Association with FtsZ
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
2012 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 51, no 7, 1407-1415 p.Article in journal (Refereed) Published
Abstract [en]

ZipA is an essential component of the cell division machinery in E. coil 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.

Place, publisher, year, edition, pages
2012. Vol. 51, no 7, 1407-1415 p.
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-76962DOI: 10.1021/bi2015647ISI: 000300473400009OAI: oai:DiVA.org:su-76962DiVA: diva2:534227
Note
2Available from: 2012-06-15 Created: 2012-05-28 Last updated: 2017-12-07Bibliographically approved

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