Replication termination in Escherichia coli: structure and antihelicase activity of the Tus-Ter complex


Neylon, Cameron, Kralicek, Andrew V., Hill, Thomas M. and Dixon, Nicholas E. (2005) Replication termination in Escherichia coli: structure and antihelicase activity of the Tus-Ter complex. Microbiology and Molecular Biology Reviews, 69, (3), 501-526. (doi:10.1128/MMBR.69.3.501-526.2005).

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Description/Abstract

The arrest of DNA replication in Escherichia coli is triggered by the encounter of a replisome with a Tus protein-Ter DNA complex. A replication fork can pass through a Tus-Ter complex when traveling in one direction but not the other, and the chromosomal Ter sites are oriented so replication forks can enter, but not exit, the terminus region. The Tus-Ter complex acts by blocking the action of the replicative DnaB helicase, but details of the mechanism are uncertain. One proposed mechanism involves a specific interaction between Tus-Ter and the helicase that prevents further DNA unwinding, while another is that the Tus-Ter complex itself is sufficient to block the helicase in apolar manner, without the need for specific protein -protein interactions. This review integrates three decades of experimental information on the action of the Tus-Ter complex with information available from the Tus-TerA crystal structure. We conclude that while it is possible to explain polar fork arrest by a mechanism involving only the Tus- Ter interaction, there are also strong indications of a role for specific Tus-DnaB interactions. The evidence suggests, therefore, that the termination system is more subtle and complex than may have been assumed. We describe some further experiments and insights that may assist in unraveling the details of this fascinating process.

Item Type: Article
ISSNs: 1092-2172 (print)
Related URLs:
Keywords: helicase dnab protein, single-stranded-dna, exhibit polar inhibition, complete genome sequence, large tumor-antigen, fork-arrest, bacillus-subtilis, terminus region, crystal-structure, binding-protein
Subjects: Q Science > QH Natural history > QH426 Genetics
Q Science > QR Microbiology
Divisions: University Structure - Pre August 2011 > School of Chemistry
ePrint ID: 20876
Date Deposited: 02 Mar 2006
Last Modified: 27 Mar 2014 18:10
Contact Email Address: D.C.Neylon@soton.ac.uk.
URI: http://eprints.soton.ac.uk/id/eprint/20876

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