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dc.contributor.authorJergic, Slobodan
dc.contributor.authorHoran, Nicholas P.
dc.contributor.authorElshenawy, Mohamed
dc.contributor.authorMason, Claire E.
dc.contributor.authorUrathamakul, Thitima
dc.contributor.authorOzawa, Kiyoshi
dc.contributor.authorRobinson, Andrew J.
dc.contributor.authorGoudsmits, Joris M H
dc.contributor.authorWang, Yao
dc.contributor.authorPan, Xuefeng
dc.contributor.authorBeck, Jennifer L.
dc.contributor.authorVan Oijen, Antoine M.
dc.contributor.authorHuber, Thomas L.
dc.contributor.authorHamdan, Samir
dc.contributor.authorDixon, Nicholas E.
dc.date.accessioned2015-08-03T11:00:13Z
dc.date.available2015-08-03T11:00:13Z
dc.date.issued2013-02-22
dc.identifier.issn02614189
dc.identifier.pmid23435564
dc.identifier.doi10.1038/emboj.2012.347
dc.identifier.urihttp://hdl.handle.net/10754/562660
dc.description.abstractProcessive DNA synthesis by the αÉ"θ core of the Escherichia coli Pol III replicase requires it to be bound to the β 2 clamp via a site in the α polymerase subunit. How the É" proofreading exonuclease subunit influences DNA synthesis by α was not previously understood. In this work, bulk assays of DNA replication were used to uncover a non-proofreading activity of É". Combination of mutagenesis with biophysical studies and single-molecule leading-strand replication assays traced this activity to a novel β-binding site in É" that, in conjunction with the site in α, maintains a closed state of the αÉ"θ-β 2 replicase in the polymerization mode of DNA synthesis. The É"-β interaction, selected during evolution to be weak and thus suited for transient disruption to enable access of alternate polymerases and other clamp binding proteins, therefore makes an important contribution to the network of protein-protein interactions that finely tune stability of the replicase on the DNA template in its various conformational states. © 2013 European Molecular Biology Organization.
dc.description.sponsorshipWe thank Michelle Blayney and Linda Jessop for preliminary ESI-MS data. This work was supported by grants from the Australian Research Council, including Fellowships to KO, TH, and NED, and by a KAUST Faculty Initiated Collaborative grant to SMH and NED.
dc.publisherWiley
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3642676
dc.subjectbeta sliding clamp
dc.subjectDNA polymerase III
dc.subjectDNA replication
dc.subjectEscherichia coli
dc.subjectproofreading exonuclease
dc.titleA direct proofreader-clamp interaction stabilizes the Pol III replicase in the polymerization mode
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentBioscience Program
dc.identifier.journalEMBO Journal
dc.identifier.pmcidPMC3642676
dc.contributor.institutionSchool of Chemistry, University of Wollongong, Northfields Avenue, Wollongong, NSW 2522, Australia
dc.contributor.institutionResearch School of Chemistry, Australian National University, Canberra, ACT, Australia
dc.contributor.institutionZernike Institute for Advanced Materials, Groningen, Netherlands
dc.contributor.institutionDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, United States
dc.contributor.institutionSchool of Life Science, Beijing Institute of Technology, Beijing 100081, China
kaust.personHamdan, Samir
kaust.personElshenawy, Mohamed


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