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 Previous Article

Microbiology and Molecular Biology Reviews, September 2005, p. 501-526, Vol. 69, No. 3
1092-2172/05/$08.00+0     doi:10.1128/MMBR.69.3.501-526.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Replication Termination in Escherichia coli: Structure and Antihelicase Activity of the Tus-Ter Complex

Cameron Neylon,1,2* Andrew V. Kralicek,2,3 Thomas M. Hill,4 and Nicholas E. Dixon2

School of Chemistry, University of Southampton, Southampton SO17 1BJ, United Kingdom,1 Research School of Chemistry, Australian National University, A.C.T. 0200, Australia,2 Gene Technologies Sector, HortResearch, Auckland, New Zealand,3 Department of Microbiology and Immunology, School of Medicine and Health Sciences, University of North Dakota, Grand Forks, North Dakota 58202-90374

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 a polar 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.

* Corresponding author. Mailing address: School of Chemistry, University of Southampton, Southampton SO17 1BJ, United Kingdom. Phone: (44) 23 8059 4164. Fax: (44) 23 8059 6805. E-mail: D.C.Neylon{at}soton.ac.uk.

Microbiology and Molecular Biology Reviews, September 2005, p. 501-526, Vol. 69, No. 3
1092-2172/05/$08.00+0     doi:10.1128/MMBR.69.3.501-526.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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