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Lookup NU author(s): Elisa Galli, Professor Kenn Gerdes
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P>FtsZ, the essential regulator of bacterial cell division, is a dynamic cytoskeletal protein that forms helices that condense into the Z-ring prior to division. Two small coiled-coil proteins, ZapA and ZapB, are both recruited early to the Z-ring. We show here that ZapB is recruited to the Z-ring by ZapA. A direct interaction between ZapA and ZapB is supported by bacterial two-hybrid and in vitro interaction assays. Using high-resolution 3-D reconstruction microscopy, we find that, surprisingly, ZapB is located inside the Z-ring in virtually all cells investigated. We propose a molecular model in which ZapA increases lateral interactions between FtsZ proto-filaments and ZapB mediates further stabilization of this interaction by cross-linking ZapA molecules bound to adjacent FtsZ proto-filaments. Gene deletion and complementation assays show that ZapB can mitigate cell division and Z-ring assembly defects even in the absence of ZapA, raising the possibility that ZapB stimulates Z-ring assembly by two different mechanisms.
Author(s): Galli E, Gerdes K
Publication type: Article
Publication status: Published
Journal: Molecular Microbiology
Year: 2010
Volume: 76
Issue: 6
Pages: 1514-1526
Print publication date: 01/06/2010
ISSN (print): 0950-382X
ISSN (electronic): 1365-2958
Publisher: Wiley-Blackwell
URL: http://dx.doi.org/10.1111/j.1365-2958.2010.07183.x
DOI: 10.1111/j.1365-2958.2010.07183.x
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