Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/32785
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dc.contributor.authorMeineke, B.-
dc.contributor.authorSchwer, B.-
dc.contributor.authorSchaffrath, Raffael-
dc.contributor.authorShuman, S.-
dc.date.accessioned2015-07-21T11:23:06Z-
dc.date.available2015-07-21T11:23:06Z-
dc.date.issued2010-09-19-
dc.identifier.citationNucleic Acids Research, 2011, 39 (2), pp. 687-700en
dc.identifier.issn0305-1048-
dc.identifier.urihttp://nar.oxfordjournals.org/content/39/2/687en
dc.identifier.urihttp://hdl.handle.net/2381/32785-
dc.description.abstracttRNA damage inflicted by the Escherichia coli anticodon nuclease PrrC (EcoPrrC) underlies an antiviral response to phage T4 infection. PrrC homologs are present in many bacterial proteomes, though their biological activities are uncharted. PrrCs consist of two domains: an N-terminal NTPase module related to the ABC family and a distinctive C-terminal ribonuclease module. In this article, we report that the expression of EcoPrrC in budding yeast is fungicidal, signifying that PrrC is toxic in a eukaryon in the absence of other bacterial or viral proteins. Whereas Streptococcus PrrC is also toxic in yeast, Neisseria and Xanthomonas PrrCs are not. Via analysis of the effects of 118 mutations on EcoPrrC toxicity in yeast, we identified 22 essential residues in the NTPase domain and 11 in the nuclease domain. Overexpressing PrrCs with mutations in the NTPase active site ameliorated the toxicity of wild-type EcoPrrC. Our findings support a model in which EcoPrrC toxicity is contingent on head-to-tail dimerization of the NTPase domains to form two composite NTP phosphohydrolase sites. Comparisons of EcoPrrC activity in a variety of yeast genetic backgrounds, and the rescuing effects of tRNA overexpression, implicate tRNA[superscript: Lys(UUU)] as a target of EcoPrrC toxicity in yeast.en
dc.language.isoenen
dc.publisherOxford University Pressen
dc.relation.urihttp://www.ncbi.nlm.nih.gov/pubmed/20855293-
dc.rightsCopyright © The Author(s) 2010. Published by Oxford University Press. This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.en
dc.subjectAlanineen
dc.subjectAmino Acid Sequenceen
dc.subjectBacterial Proteinsen
dc.subjectBacterial Toxinsen
dc.subjectEscherichia coli Proteinsen
dc.subjectMolecular Sequence Dataen
dc.subjectMutagenesisen
dc.subjectProtein Structure, Tertiaryen
dc.subjectRNA, Transferen
dc.subjectRNA, Transfer, Lysen
dc.subjectRibonucleasesen
dc.subjectSaccharomyces cerevisiaeen
dc.subjectSequence Homology, Amino Aciden
dc.subjectStructure-Activity Relationshipen
dc.titleDeterminants of eukaryal cell killing by the bacterial ribotoxin PrrCen
dc.typeJournal Articleen
dc.identifier.doi10.1093/nar/gkq831-
dc.identifier.eissn1362-4962-
dc.identifier.piigkq831-
dc.description.statusPeer-revieweden
dc.description.versionPublisher Versionen
dc.type.subtypeJournal Article;Research Support, N.I.H., Extramural-
pubs.organisational-group/Organisationen
pubs.organisational-group/Organisation/COLLEGE OF MEDICINE, BIOLOGICAL SCIENCES AND PSYCHOLOGYen
pubs.organisational-group/Organisation/COLLEGE OF MEDICINE, BIOLOGICAL SCIENCES AND PSYCHOLOGY/School of Biological Sciencesen
pubs.organisational-group/Organisation/COLLEGE OF MEDICINE, BIOLOGICAL SCIENCES AND PSYCHOLOGY/School of Biological Sciences/Department of Geneticsen
dc.dateaccepted2010-09-03-
Appears in Collections:Published Articles, Dept. of Genetics

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