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Substrate Recognition and Autoinhibition in the Central Ribonuclease RNase E.

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cam.issuedOnline2018-09-27
dc.contributor.authorBandyra, Katarzyna J
dc.contributor.authorWandzik, Joanna M
dc.contributor.authorLuisi, Ben F
dc.contributor.orcidBandyra, Katarzyna [0000-0003-2607-6700]
dc.contributor.orcidLuisi, Ben [0000-0003-1144-9877]
dc.date.accessioned2018-11-07T00:30:38Z
dc.date.available2018-11-07T00:30:38Z
dc.date.issued2018-10-18
dc.description.abstractThe endoribonuclease RNase E is a principal factor in RNA turnover and processing that helps to exercise fine control of gene expression in bacteria. While its catalytic activity can be strongly influenced by the chemical identity of the 5' end of RNA substrates, the enzyme can also cleave numerous substrates irrespective of the chemistry of their 5' ends through a mechanism that has remained largely unexplained. We report structural and functional data illuminating details of both operational modes. Our crystal structure of RNase E in complex with the sRNA RprA reveals a duplex recognition site that saddles an inter-protomer surface to help present substrates for cleavage. Our data also reveal an autoinhibitory pocket that modulates the overall activity of the ribonuclease. Taking these findings together, we propose how RNase E uses versatile modes of RNA recognition to achieve optimal activity and specificity.
dc.description.sponsorshipWellcome Trust
dc.format.mediumPrint-Electronic
dc.identifier.doi10.17863/CAM.32060
dc.identifier.eissn1097-4164
dc.identifier.issn1097-2765
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/284687
dc.languageeng
dc.language.isoeng
dc.publisherElsevier BV
dc.publisher.urlhttp://dx.doi.org/10.1016/j.molcel.2018.08.039
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectRNA degradation
dc.subjectRNA processing
dc.subjectRNA structure
dc.subjectRNA-mediated regulation
dc.subjectRNase E
dc.subjectprotein-RNA interactions
dc.subjectprotein-RNA structure
dc.subjectsmall regulatory RNA
dc.subjectAmino Acid Sequence
dc.subjectCatalysis
dc.subjectEndoribonucleases
dc.subjectEscherichia coli
dc.subjectEscherichia coli Proteins
dc.subjectGene Expression Regulation, Bacterial
dc.subjectProtein Subunits
dc.subjectRNA
dc.subjectRNA, Bacterial
dc.subjectSequence Alignment
dc.subjectSubstrate Specificity
dc.titleSubstrate Recognition and Autoinhibition in the Central Ribonuclease RNase E.
dc.typeArticle
dcterms.dateAccepted2018-08-24
prism.endingPage285.e4
prism.issueIdentifier2
prism.publicationDate2018
prism.publicationNameMol Cell
prism.startingPage275
prism.volume72
pubs.funder-project-idWellcome Trust (200873/Z/16/Z)
rioxxterms.licenseref.startdate2018-10
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.typeJournal Article/Review
rioxxterms.versionVoR
rioxxterms.versionofrecord10.1016/j.molcel.2018.08.039

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