PMID:21113127

Citation	Tonthat, NK, Arold, ST, Pickering, BF, Van Dyke, MW, Liang, S, Lu, Y, Beuria, TK, Margolin, W and Schumacher, MA (2011) Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check.EMBO J. 30:154-64
Abstract	In Escherichia coli, cytokinesis is orchestrated by FtsZ, which forms a Z-ring to drive septation. Spatial and temporal control of Z-ring formation is achieved by the Min and nucleoid occlusion (NO) systems. Unlike the well-studied Min system, less is known about the anti-DNA guillotining NO process. Here, we describe studies addressing the molecular mechanism of SlmA (synthetic lethal with a defective Min system)-mediated NO. SlmA contains a TetR-like DNA-binding fold, and chromatin immunoprecipitation analyses show that SlmA-binding sites are dispersed on the chromosome except the Ter region, which segregates immediately before septation. SlmA binds DNA and FtsZ simultaneously, and the SlmA-FtsZ structure reveals that two FtsZ molecules sandwich a SlmA dimer. In this complex, FtsZ can still bind GTP and form protofilaments, but the separated protofilaments are forced into an anti-parallel arrangement. This suggests that SlmA may alter FtsZ polymer assembly. Indeed, electron microscopy data, showing that SlmA-DNA disrupts the formation of normal FtsZ polymers and induces distinct spiral structures, supports this. Thus, the combined data reveal how SlmA derails Z-ring formation at the correct place and time to effect NO.
Links	PubMed Online version:10.1038/emboj.2010.288
Keywords	Bacterial Proteins; Base Sequence; Binding Sites; Carrier Proteins; Chromosomes, Bacterial; Crystallography, X-Ray; Cytokinesis; Cytoskeletal Proteins; DNA, Bacterial; Escherichia coli; Escherichia coli Proteins; Models, Molecular; Protein Binding; Protein Conformation; Protein Multimerization; Scattering, Small Angle; X-Ray Diffraction
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Species	Taxon ID	Strain	Gene (if known)	OMP	Phenotype	Details	Evidence	Notes
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