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dc.contributor.authorKrajewski, WWen_US
dc.contributor.authorFu, Xen_US
dc.contributor.authorWilkinson, Men_US
dc.contributor.authorCronin, NBen_US
dc.contributor.authorDillingham, MSen_US
dc.contributor.authorWigley, DBen_US
dc.date.accessioned2018-11-29T09:21:02Z
dc.date.issued2014-04en_US
dc.identifier.citationNature, 2014, 508 (7496), pp. 416 - 419en_US
dc.identifier.issn0028-0836en_US
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/2963
dc.identifier.eissn1476-4687en_US
dc.identifier.doi10.1038/nature13037en_US
dc.description.abstractIn bacterial cells, processing of double-stranded DNA breaks for repair by homologous recombination is dependent upon the recombination hotspot sequence χ (Chi) and is catalysed by either an AddAB- or RecBCD-type helicase-nuclease (reviewed in refs 3, 4). These enzyme complexes unwind and digest the DNA duplex from the broken end until they encounter a χ sequence, whereupon they produce a 3' single-stranded DNA tail onto which they initiate loading of the RecA protein. Consequently, regulation of the AddAB/RecBCD complex by χ is a key control point in DNA repair and other processes involving genetic recombination. Here we report crystal structures of Bacillus subtilis AddAB in complex with different χ-containing DNA substrates either with or without a non-hydrolysable ATP analogue. Comparison of these structures suggests a mechanism for DNA translocation and unwinding, suggests how the enzyme binds specifically to χ sequences, and explains how χ recognition leads to the arrest of AddAB (and RecBCD) translocation that is observed in single-molecule experiments.en_US
dc.formatPrint-Electronicen_US
dc.format.extent416 - 419en_US
dc.languageengen_US
dc.language.isoengen_US
dc.rights.urihttp://www.rioxx.net/licenses/all-rights-reserveden_US
dc.subjectBacillus subtilisen_US
dc.subjectExodeoxyribonucleasesen_US
dc.subjectDNA Helicasesen_US
dc.subjectBacterial Proteinsen_US
dc.subjectDNAen_US
dc.subjectAdenosine Triphosphateen_US
dc.subjectCrystallography, X-Rayen_US
dc.subjectRecombination, Geneticen_US
dc.subjectBinding Sitesen_US
dc.subjectMolecular Conformationen_US
dc.subjectStructure-Activity Relationshipen_US
dc.subjectModels, Molecularen_US
dc.titleStructural basis for translocation by AddAB helicase-nuclease and its arrest at χ sites.en_US
dc.typeJournal Article
dcterms.dateAccepted2014-01-16en_US
rioxxterms.versionofrecord10.1038/nature13037en_US
rioxxterms.licenseref.startdate2014-04en_US
rioxxterms.typeJournal Article/Reviewen_US
dc.relation.isPartOfNatureen_US
pubs.issue7496en_US
pubs.notesNot knownen_US
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Closed research teams
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Closed research teams/Wigley Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology/Structural Electron Microscopy
pubs.volume508en_US
pubs.embargo.termsNot knownen_US
icr.researchteamWigley Groupen_US
icr.researchteamStructural Electron Microscopyen_US
dc.contributor.icrauthorWigley, Dale Brianen_US
dc.contributor.icrauthorFu, Xinen_US


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