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dc.contributor.authorCole, Sarah E.
dc.contributor.authorlaRiviere, Frederick J.
dc.contributor.authorlaRiviere, Frederick J.
dc.contributor.authorMerrikh, Christopher N.
dc.contributor.authorMoore, Melissa J.
dc.contributor.authorMerrikh, Christopher N.
dc.contributor.authorMoore, Melissa J.
dc.date2022-08-11T08:08:54.000
dc.date.accessioned2022-08-23T16:11:53Z
dc.date.available2022-08-23T16:11:53Z
dc.date.issued2009-05-14
dc.date.submitted2013-03-18
dc.identifier.citationMol Cell. 2009 May 14;34(4):440-50. doi: 10.1016/j.molcel.2009.04.017. <a href="http://dx.doi.org/10.1016/j.molcel.2009.04.017">Link to article on publisher's site</a>
dc.identifier.issn1097-2765 (Linking)
dc.identifier.doi10.1016/j.molcel.2009.04.017
dc.identifier.pmid19481524
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33273
dc.description.abstractEukaryotes possess numerous quality control systems that monitor both the synthesis of RNA and the integrity of the finished products. We previously demonstrated that Saccharomyces cerevisiae possesses a quality control mechanism, nonfunctional rRNA decay (NRD), capable of detecting and eliminating translationally defective rRNAs. Here we show that NRD can be divided into two mechanistically distinct pathways: one that eliminates rRNAs with deleterious mutations in the decoding site (18S NRD) and one that eliminates rRNAs containing deleterious mutations in the peptidyl transferase center (25S NRD). 18S NRD is dependent on translation elongation and utilizes the same proteins as those participating in no-go mRNA decay (NGD). In cells that accumulate 18S NRD and NGD decay intermediates, both RNA types can be seen in P-bodies. We propose that 18S NRD and NGD are different observable outcomes of the same initiating event: a ribosome stalled inappropriately at a sense codon during translation elongation.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=19481524&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1016/j.molcel.2009.04.017
dc.subjectAdaptor Proteins, Signal Transducing; Animals; Biological Markers; Cell Nucleus; Exoribonucleases; GTP-Binding Proteins; HSP70 Heat-Shock Proteins; Humans; In Situ Hybridization, Fluorescence; Peptide Elongation Factors; *RNA Stability; *RNA, Messenger; *RNA, Ribosomal; *RNA, Ribosomal, 18S; *Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins
dc.subjectGenetics and Genomics
dc.subjectMolecular Biology
dc.titleA convergence of rRNA and mRNA quality control pathways revealed by mechanistic analysis of nonfunctional rRNA decay
dc.typeJournal Article
dc.source.journaltitleMolecular cell
dc.source.volume34
dc.source.issue4
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/1805
dc.identifier.contextkey3920181
html.description.abstract<p>Eukaryotes possess numerous quality control systems that monitor both the synthesis of RNA and the integrity of the finished products. We previously demonstrated that Saccharomyces cerevisiae possesses a quality control mechanism, nonfunctional rRNA decay (NRD), capable of detecting and eliminating translationally defective rRNAs. Here we show that NRD can be divided into two mechanistically distinct pathways: one that eliminates rRNAs with deleterious mutations in the decoding site (18S NRD) and one that eliminates rRNAs containing deleterious mutations in the peptidyl transferase center (25S NRD). 18S NRD is dependent on translation elongation and utilizes the same proteins as those participating in no-go mRNA decay (NGD). In cells that accumulate 18S NRD and NGD decay intermediates, both RNA types can be seen in P-bodies. We propose that 18S NRD and NGD are different observable outcomes of the same initiating event: a ribosome stalled inappropriately at a sense codon during translation elongation.</p>
dc.identifier.submissionpathgsbs_sp/1805
dc.contributor.departmentGraduate School of Biomedical Sciences, Biochemistry and Molecular Pharmacology Program
dc.source.pages440-50
dc.contributor.studentChristopher Merrikh


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