Replisome speed determines the efficiency of the Tus-Ter replication termination barrier (Q27702035)

8

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Aaron J. Oakley

object named as

Aaron J Oakley

6

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Nicholas E. Dixon

object named as

Nicholas E Dixon

7

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author name string

Slobodan Jergic

2

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Zhi-Qiang Xu

3

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Mohamed A Sobhy

4

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Masateru Takahashi

Structure of a replication-terminator protein complexed with DNA

5

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language of work or name

English

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publication date

17 September 2015

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published in

Nature

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volume

525

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issue

7569

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page(s)

394-8

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cites work

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Replication termination mechanism as revealed by Tus-mediated polar arrest of a sliding helicase

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Molecular traffic jams on DNA

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Refinement of macromolecular structures by the maximum-likelihood method

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Features and development of Coot

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Entropic elasticity of lambda-phage DNA

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MOLREP: an Automated Program for Molecular Replacement

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Use of TLS parameters to model anisotropic displacements in macromolecular refinement

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Random and site-specific replication termination.

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The terminus region of the Escherichia coli chromosome contains two separate loci that exhibit polar inhibition of replication

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

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The replication fork trap and termination of chromosome replication

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A molecular mousetrap determines polarity of termination of DNA replication in E. coli

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Mechanisms of polar arrest of a replication fork

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Tus-mediated arrest of DNA replication in Escherichia coli is modulated by DNA supercoiling

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Termination structures in the Escherichia coli chromosome replication fork trap

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DNA primase acts as a molecular brake in DNA replication

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A direct proofreader-clamp interaction stabilizes the Pol III replicase in the polymerization mode

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Real-time single-molecule observation of rolling-circle DNA replication

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Dynamics of DNA replication loops reveal temporal control of lagging-strand synthesis

21 January 2018

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Single-molecule analysis reveals that the lagging strand increases replisome processivity but slows replication fork progression

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1 reference

A single-molecule approach to DNA replication in Escherichia coli cells demonstrated that DNA polymerase III is a major determinant of fork speed.

21 January 2018

1 reference

Differential Tus-Ter binding and lock formation: implications for DNA replication termination in Escherichia coli.

21 January 2018

1 reference

Interaction of the Escherichia coli replication terminator protein (Tus) with DNA: a model derived from DNA-binding studies of mutant proteins by surface plasmon resonance

21 January 2018

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DnaB helicase activity is modulated by DNA geometry and force

21 January 2018

1 reference

Coupling of a replicative polymerase and helicase: a tau-DnaB interaction mediates rapid replication fork movement

21 January 2018

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Flexibility revealed by the 1.85 A crystal structure of the beta sliding-clamp subunit of Escherichia coli DNA polymerase III

21 January 2018

1 reference

Blu-Ice and the Distributed Control System: software for data acquisition and instrument control at macromolecular crystallography beamlines

21 January 2018

1 reference

Processing of X-ray diffraction data collected in oscillation mode

21 January 2018

1 reference

Two mechanisms coordinate replication termination by the Escherichia coli Tus-Ter complex

21 January 2018

1 reference

Single-molecule kinetics of lambda exonuclease reveal base dependence and dynamic disorder

21 January 2018

1 reference

Phi X174-type primosomal proteins: purification and assay

21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/26322585

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Sequence-specific Interactions in the Tus-Ter Complex and the Effect of Base Pair Substitutions on Arrest of DNA Replication in Escherichia coli

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/26322585

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Biophysical characteristics of Tus, the replication arrest protein of Escherichia coli

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/26322585