PMID:20487275
| Citation |
Galli, E and Gerdes, K (2010) Spatial resolution of two bacterial cell division proteins: ZapA recruits ZapB to the inner face of the Z-ring. Mol. Microbiol. 76:1514-26 |
|---|---|
| Abstract |
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. |
| Links |
PubMed Online version:10.1111/j.1365-2958.2010.07183.x |
| Keywords |
Bacterial Proteins/analysis; Carrier Proteins/analysis; Cell Cycle Proteins/analysis; Cell Division; Cytoskeletal Proteins/analysis; Escherichia coli/chemistry; Escherichia coli/physiology; Escherichia coli Proteins/analysis; Gene Deletion; Genetic Complementation Test; Imaging, Three-Dimensional; Microscopy; Models, Biological; Protein Binding |
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