dc.contributor.author | Krajewski, WW | |
dc.contributor.author | Fu, X | |
dc.contributor.author | Wilkinson, M | |
dc.contributor.author | Cronin, NB | |
dc.contributor.author | Dillingham, MS | |
dc.contributor.author | Wigley, DB | |
dc.date.accessioned | 2018-11-29T09:21:02Z | |
dc.date.issued | 2014-04-17 | |
dc.identifier.citation | Nature, 2014, 508 (7496), pp. 416 - 419 | |
dc.identifier.issn | 0028-0836 | |
dc.identifier.uri | https://repository.icr.ac.uk/handle/internal/2963 | |
dc.identifier.eissn | 1476-4687 | |
dc.identifier.doi | 10.1038/nature13037 | |
dc.description.abstract | In 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. | |
dc.format | Print-Electronic | |
dc.format.extent | 416 - 419 | |
dc.language | eng | |
dc.language.iso | eng | |
dc.publisher | NATURE PUBLISHING GROUP | |
dc.rights.uri | https://www.rioxx.net/licenses/all-rights-reserved | |
dc.subject | Bacillus subtilis | |
dc.subject | Exodeoxyribonucleases | |
dc.subject | DNA Helicases | |
dc.subject | Bacterial Proteins | |
dc.subject | DNA | |
dc.subject | Adenosine Triphosphate | |
dc.subject | Crystallography, X-Ray | |
dc.subject | Recombination, Genetic | |
dc.subject | Binding Sites | |
dc.subject | Molecular Conformation | |
dc.subject | Structure-Activity Relationship | |
dc.subject | Models, Molecular | |
dc.title | Structural basis for translocation by AddAB helicase-nuclease and its arrest at χ sites. | |
dc.type | Journal Article | |
dcterms.dateAccepted | 2014-01-16 | |
rioxxterms.versionofrecord | 10.1038/nature13037 | |
rioxxterms.licenseref.uri | https://www.rioxx.net/licenses/all-rights-reserved | |
rioxxterms.licenseref.startdate | 2014-04 | |
rioxxterms.type | Journal Article/Review | |
dc.relation.isPartOf | Nature | |
pubs.issue | 7496 | |
pubs.notes | Not known | |
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.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.publication-status | Published | |
pubs.volume | 508 | |
pubs.embargo.terms | Not known | |
icr.researchteam | Wigley Group | |
icr.researchteam | Structural Electron Microscopy | |
dc.contributor.icrauthor | Fu, Xin | |
dc.contributor.icrauthor | Wigley, Dale Brian | |