期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 292, 期 9, 页码 3740-3750出版社
ELSEVIER
DOI: 10.1074/jbc.M116.773192
关键词
cell division; cytokinesis; electron microscopy (EM); protein-protein interaction; X-ray crystallography; FtsZ; ZapD
资金
- NIGMS
- National Institutes of Health
- Howard Hughes Medical Institute
- Office of Science, Office of Basic Energy Sciences, of the United States Department of Energy [DE-AC02-05CH11231]
- Sandler Foundation [MR-15-328599]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1615858] Funding Source: National Science Foundation
Cell division in most bacteria is mediated by the tubulin-like FtsZ protein, which polymerizes in a GTP-dependent manner to form the cytokinetic Z ring. A diverse repertoire of FtsZ-binding proteins affects FtsZ localization and polymerization to ensure correct Z ring formation. Many of these proteins bind the C-terminal domain (CTD) of FtsZ, which serves as a hub for FtsZ regulation. FtsZ ring-associated proteins, ZapA-D (Zaps), are important FtsZ regulatory proteins that stabilize FtsZ assembly and enhance Z ring formation by increasing lateral assembly of FtsZ protofilaments, which then form the Z ring. There are no structures of a Zap protein bound to FtsZ; therefore, how these proteins affect FtsZ polymerization has been unclear. Recent data showed ZapD binds specifically to the FtsZ CTD. Thus, to obtain insight into the ZapD-CTD interaction and how it may mediate FtsZ protofilament assembly, we determined the Escherichia coli ZapD-FtsZ CTD structure to 2.67 resolution. The structure shows that the CTD docks within a hydrophobic cleft in the ZapD helical domain and adopts an unusual structure composed of two turns of helix separated by a proline kink. FtsZ CTD residue Phe-377 inserts into the ZapD pocket, anchoring the CTD in place and permitting hydrophobic contacts between FtsZ residues Ile-374, Pro-375, and Leu-378 with ZapD residues Leu-74, Trp-77, Leu-91, and Leu-174. The structural findings were supported by mutagenesis coupled with biochemical and in vivo studies. The combined data suggest that ZapD acts as a molecular cross-linking reagent between FtsZ protofilaments to enhance FtsZ assembly.
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