Single-molecule visualization of stalled replication-fork rescue by the Escherichia coli Rep helicase
Author:
Affiliation:
1. Molecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong , Wollongong , New South Wales 2522, Australia
2. Illawarra Health & Medical Research Institute , Wollongong , New South Wales 2522, Australia
Abstract
Funder
NIH
Australian Research Council
Australian Government Research Training Program Scholarship
Publisher
Oxford University Press (OUP)
Subject
Genetics
Link
https://academic.oup.com/nar/article-pdf/51/7/3307/49875805/gkad186.pdf
Reference76 articles.
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2. DNA polymerase III holoenzyme of Escherichia coli. II. A novel complex including the γ subunit essential for processive synthesis;Maki;J. Biol. Chem.,1988
3. A direct proofreader-clamp interaction stabilizes the Pol III replicase in the polymerization mode;Jergic;EMBO J.,2013
4. Replisome speed determines the efficiency of the Tus-Ter replication termination barrier;Elshenawy;Nature,2015
5. A single-molecule approach to DNA replication in Escherichia coli cells demonstrated that DNA polymerase III is a major determinant of fork speed;Pham;Mol. Microbiol.,2013
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