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Molecular basis for a protein-mediated DNA-bridging mechanism that functions in condensation of the E. coli chromosome.

Publication ,  Journal Article
Dupaigne, P; Tonthat, NK; Espéli, O; Whitfill, T; Boccard, F; Schumacher, MA
Published in: Mol Cell
November 30, 2012

The E. coli chromosome is condensed into insulated regions termed macrodomains (MDs), which are essential for genomic packaging. How chromosomal MDs are specifically organized and compacted is unknown. Here, we report studies revealing the molecular basis for Terminus-containing (Ter) chromosome condensation by the Ter-specific factor MatP. MatP contains a tripartite fold with a four-helix bundle DNA-binding motif, ribbon-helix-helix and C-terminal coiled-coil. Strikingly, MatP-matS structures show that the MatP coiled-coils form bridged tetramers that flexibly link distant matS sites. Atomic force microscopy and electron microscopy studies demonstrate that MatP alone loops DNA. Mutation of key coiled-coil residues destroys looping and causes a loss of Ter condensation in vivo. Thus, these data reveal the molecular basis for a protein-mediated DNA-bridging mechanism that mediates condensation of a large chromosomal domain in enterobacteria.

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Published In

Mol Cell

DOI

EISSN

1097-4164

Publication Date

November 30, 2012

Volume

48

Issue

4

Start / End Page

560 / 571

Location

United States

Related Subject Headings

  • Protein Binding
  • Models, Molecular
  • Microscopy, Electron
  • Microscopy, Atomic Force
  • Escherichia coli Proteins
  • Escherichia coli K12
  • Developmental Biology
  • DNA, Bacterial
  • Chromosomes, Bacterial
  • Chromosomal Proteins, Non-Histone
 

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Dupaigne, P., Tonthat, N. K., Espéli, O., Whitfill, T., Boccard, F., & Schumacher, M. A. (2012). Molecular basis for a protein-mediated DNA-bridging mechanism that functions in condensation of the E. coli chromosome. Mol Cell, 48(4), 560–571. https://doi.org/10.1016/j.molcel.2012.09.009
Dupaigne, Pauline, Nam K. Tonthat, Olivier Espéli, Travis Whitfill, Frédéric Boccard, and Maria A. Schumacher. “Molecular basis for a protein-mediated DNA-bridging mechanism that functions in condensation of the E. coli chromosome.Mol Cell 48, no. 4 (November 30, 2012): 560–71. https://doi.org/10.1016/j.molcel.2012.09.009.
Dupaigne P, Tonthat NK, Espéli O, Whitfill T, Boccard F, Schumacher MA. Molecular basis for a protein-mediated DNA-bridging mechanism that functions in condensation of the E. coli chromosome. Mol Cell. 2012 Nov 30;48(4):560–71.
Dupaigne, Pauline, et al. “Molecular basis for a protein-mediated DNA-bridging mechanism that functions in condensation of the E. coli chromosome.Mol Cell, vol. 48, no. 4, Nov. 2012, pp. 560–71. Pubmed, doi:10.1016/j.molcel.2012.09.009.
Dupaigne P, Tonthat NK, Espéli O, Whitfill T, Boccard F, Schumacher MA. Molecular basis for a protein-mediated DNA-bridging mechanism that functions in condensation of the E. coli chromosome. Mol Cell. 2012 Nov 30;48(4):560–571.
Journal cover image

Published In

Mol Cell

DOI

EISSN

1097-4164

Publication Date

November 30, 2012

Volume

48

Issue

4

Start / End Page

560 / 571

Location

United States

Related Subject Headings

  • Protein Binding
  • Models, Molecular
  • Microscopy, Electron
  • Microscopy, Atomic Force
  • Escherichia coli Proteins
  • Escherichia coli K12
  • Developmental Biology
  • DNA, Bacterial
  • Chromosomes, Bacterial
  • Chromosomal Proteins, Non-Histone