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Spatial resolution of two bacterial cell division proteins: ZapA recruits ZapB to the inner face of the Z-ring

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.

Publication metadata

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


DOI: 10.1111/j.1365-2958.2010.07183.x


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