Medical Journals

A Molecular Mousetrap Determines Polarity of Termination of Dna Replication in E. Coli.

Authors:
  • Mulcair Mark D
  • Schaeffer Patrick M
  • Oakley Aaron J
  • Cross Hannah F
  • Neylon Cameron
  • Hill Thomas M
  • Dixon Nicholas E

From: Research School of Chemistry, Australian National University, Canberra, ACT 0200, Australia.

Cell

  • Publish Date: Jun 2006
  • ISSN: 0092-8674
  • Volume: 125
  • Issue: 7
  • Pages: 1309-19
  • Medium: Print
  • Language: English
  • Citation (JAMA): Mulcair Mark D, Schaeffer Patrick M, Oakley Aaron J, et al. A Molecular Mousetrap Determines Polarity of Termination of Dna Replication in E. Coli.. Cell Jun 2006;125:1309-19

Abstract

During chromosome synthesis in Escherichia coli, replication forks are blocked by Tus bound Ter sites on approach from one direction but not the other. To study the basis of this polarity, we measured the rates of dissociation of Tus from forked TerB oligonucleotides, such as would be produced by the replicative DnaB helicase at both the fork-blocking (nonpermissive) and permissive ends of the Ter site. Strand separation of a few nucleotides at the permissive end was sufficient to force rapid dissociation of Tus to allow fork progression. In contrast, strand separation extending to and including the strictly conserved G-C(6) base pair at the nonpermissive end led to formation of a stable locked complex. Lock formation specifically requires the cytosine residue, C(6). The crystal structure of the locked complex showed that C(6) moves 14 A from its normal position to bind in a cytosine-specific pocket on the surface of Tus.

Mesh Headings (Keywords): Adenosine Triphosphatases, Animals, Base Pairing, Base Sequence, Binding Sites, Buffers, Crystallography, X-Ray, DNA Helicases, DNA Replication, DNA, Bacterial, DNA-Binding Proteins, DnaB Helicases, Escherichia coli, Escherichia coli Proteins, Glutamates, Kinetics, Mice, Models, Biological, Models, Molecular, Multiprotein Complexes, Mutation, Replication Origin, Surface Plasmon Resonance, Thermodynamics


Check for Full Text / PubMed Unique Identifier (PMID): 16814717


This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.

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The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.


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