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dc.contributor.authorPei, Xueen
dc.contributor.authorBralley, Patriciaen
dc.contributor.authorJones, George Hen
dc.contributor.authorLuisi, Benen
dc.date.accessioned2015-09-08T10:44:41Z
dc.date.available2015-09-08T10:44:41Z
dc.date.issued2015-08-07en
dc.identifier.citationNucleic Acids Research 2015, 43(16), 8066-8076. doi: 10.1093/nar/gkv732en
dc.identifier.issn0305-1048
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/250530
dc.description.abstractIn diverse bacterial species, the turnover and processing of many RNAs is mediated by the ribonuclease RNase J, a member of the widely occurring metallo-β-lactamase enzyme family. We present crystal structures of Streptomyces coelicolor RNase J with bound RNA in pre- and post-cleavage states, at 2.27 Å and 2.80 Å resolution, respectively. These structures reveal snapshots of the enzyme cleaving substrate directionally and sequentially from the 5′ terminus. In the pre-cleavage state, a water molecule is coordinated to a zinc ion pair in the active site but is imperfectly oriented to launch a nucleophilic attack on the phosphate backbone. A conformational switch is envisaged that enables the in-line positioning of the attacking water and may be facilitated by magnesium ions. Adjacent to the scissile bond, four bases are stacked in a tightly sandwiching pocket, and mutagenesis results indicate that this organization helps to drive processive exo-ribonucleolytic cleavage. Like its numerous homologues, S. coelicolor RNase J can also cleave some RNA internally, and the structural data suggest how the preference for exo- versus endo-cleavage mode is linked with recognition of the chemical status of the substrate's 5′ end.
dc.description.sponsorshipB.F.L. and X.Y.P. are supported by the Wellcome Trust.
dc.languageEnglishen
dc.language.isoenen
dc.publisherOxford University Press
dc.titleLinkage of catalysis and 5' end recognition in ribonuclease RNase Jen
dc.typeArticle
dc.description.versionThis is the final version of the article. It first appeared from Oxford University Press via http://dx.doi.org/10.1093/nar/gkv732en
prism.endingPage8076
prism.publicationDate2015en
prism.publicationNameNucleic Acids Researchen
prism.startingPage8066
prism.volume43en
dc.rioxxterms.funderWellcome Trust
dc.rioxxterms.projectid076846/Z/05/A
dcterms.dateAccepted2015-07-07en
rioxxterms.versionofrecord10.1093/nar/gkv732en
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserveden
rioxxterms.licenseref.startdate2015-08-07en
dc.contributor.orcidLuisi, Ben [0000-0003-1144-9877]
dc.identifier.eissn1362-4962
rioxxterms.typeJournal Article/Reviewen
pubs.funder-project-idWellcome Trust (076846/Z/05/A)
pubs.funder-project-idWellcome Trust (076846/Z/05/B)


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