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Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check.

Publication ,  Journal Article
Tonthat, NK; Arold, ST; Pickering, BF; Van Dyke, MW; Liang, S; Lu, Y; Beuria, TK; Margolin, W; Schumacher, MA
Published in: EMBO J
January 5, 2011

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.

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Published In

EMBO J

DOI

EISSN

1460-2075

Publication Date

January 5, 2011

Volume

30

Issue

1

Start / End Page

154 / 164

Location

England

Related Subject Headings

  • X-Ray Diffraction
  • Scattering, Small Angle
  • Protein Multimerization
  • Protein Conformation
  • Protein Binding
  • Models, Molecular
  • Escherichia coli Proteins
  • Escherichia coli
  • Developmental Biology
  • DNA, Bacterial
 

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Tonthat, N. K., Arold, S. T., Pickering, B. F., Van Dyke, M. W., Liang, S., Lu, Y., … Schumacher, M. A. (2011). Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check. EMBO J, 30(1), 154–164. https://doi.org/10.1038/emboj.2010.288
Tonthat, Nam Ky, Stefan T. Arold, Brian F. Pickering, Michael W. Van Dyke, Shoudan Liang, Yue Lu, Tushar K. Beuria, William Margolin, and Maria A. Schumacher. “Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check.EMBO J 30, no. 1 (January 5, 2011): 154–64. https://doi.org/10.1038/emboj.2010.288.
Tonthat NK, Arold ST, Pickering BF, Van Dyke MW, Liang S, Lu Y, et al. Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check. EMBO J. 2011 Jan 5;30(1):154–64.
Tonthat, Nam Ky, et al. “Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check.EMBO J, vol. 30, no. 1, Jan. 2011, pp. 154–64. Pubmed, doi:10.1038/emboj.2010.288.
Tonthat NK, Arold ST, Pickering BF, Van Dyke MW, Liang S, Lu Y, Beuria TK, Margolin W, Schumacher MA. Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check. EMBO J. 2011 Jan 5;30(1):154–164.

Published In

EMBO J

DOI

EISSN

1460-2075

Publication Date

January 5, 2011

Volume

30

Issue

1

Start / End Page

154 / 164

Location

England

Related Subject Headings

  • X-Ray Diffraction
  • Scattering, Small Angle
  • Protein Multimerization
  • Protein Conformation
  • Protein Binding
  • Models, Molecular
  • Escherichia coli Proteins
  • Escherichia coli
  • Developmental Biology
  • DNA, Bacterial