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http://purl.uniprot.org/citations/18713869http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18713869http://www.w3.org/2000/01/rdf-schema#comment"Ribonuclease P (RNase P) is an essential endonuclease responsible for the 5'-end maturation of precursor tRNAs. Bacterial RNase P also processes precursor 4.5S RNA, tmRNA, 30S preribosomal RNA, and several reported protein-coding RNAs. Eukaryotic nuclear RNase P is far more complex than in the bacterial form, employing multiple essential protein subunits in addition to the catalytic RNA subunit. RNomic studies have shown that RNase P binds other RNAs in addition to tRNAs, but no non-tRNA substrates have previously been identified. Additional substrates were identified by using a multipronged approach in the budding yeast Saccharomyces cerevisiae. First, RNase P-dependant changes in RNA abundance were examined on whole-genome microarrays by using strains containing temperature sensitive (TS) mutations in two of the essential RNase P subunits, Pop1p and Rpr1r. Second, RNase P was rapidly affinity-purified, and copurified RNAs were identified by using a genome-wide microarray. Third, to identify RNAs that do not change abundance when RNase P is depleted but accumulate as larger precursors, >80 potential small RNA substrates were probed directly by Northern blot analysis with RNA from the RNase P TS mutants. Numerous potential substrates were identified, of which we characterized the box C/D intron-encoded small nucleolar RNAs (snoRNAs), because these both copurify with RNase P and accumulate larger forms in the RNase P temperature-sensitive mutants. It was previously known that two pathways existed for excising these snoRNAs, one using the pre-mRNA splicing path and the other that was independent of splicing. RNase P appears to participate in the splicing-independent path for the box C/D intron-encoded snoRNAs."xsd:string
http://purl.uniprot.org/citations/18713869http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0801906105"xsd:string
http://purl.uniprot.org/citations/18713869http://purl.uniprot.org/core/author"Pleiss J.A."xsd:string
http://purl.uniprot.org/citations/18713869http://purl.uniprot.org/core/author"Whitworth G.B."xsd:string
http://purl.uniprot.org/citations/18713869http://purl.uniprot.org/core/author"Engelke D.R."xsd:string
http://purl.uniprot.org/citations/18713869http://purl.uniprot.org/core/author"Coughlin D.J."xsd:string
http://purl.uniprot.org/citations/18713869http://purl.uniprot.org/core/author"Walker S.C."xsd:string
http://purl.uniprot.org/citations/18713869http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18713869http://purl.uniprot.org/core/name"Proc Natl Acad Sci U S A"xsd:string
http://purl.uniprot.org/citations/18713869http://purl.uniprot.org/core/pages"12218-12223"xsd:string
http://purl.uniprot.org/citations/18713869http://purl.uniprot.org/core/title"Genome-wide search for yeast RNase P substrates reveals role in maturation of intron-encoded box C/D small nucleolar RNAs."xsd:string
http://purl.uniprot.org/citations/18713869http://purl.uniprot.org/core/volume"105"xsd:string
http://purl.uniprot.org/citations/18713869http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18713869
http://purl.uniprot.org/citations/18713869http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18713869
http://purl.uniprot.org/uniprot/P38291#attribution-E051AE176AF017BB56A121A74CD8D98Ahttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18713869
http://purl.uniprot.org/uniprot/P28005#attribution-E051AE176AF017BB56A121A74CD8D98Ahttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18713869
http://purl.uniprot.org/uniprot/P53833#attribution-E051AE176AF017BB56A121A74CD8D98Ahttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18713869
http://purl.uniprot.org/uniprot/P38336#attribution-E051AE176AF017BB56A121A74CD8D98Ahttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18713869
http://purl.uniprot.org/uniprot/P38208#attribution-E051AE176AF017BB56A121A74CD8D98Ahttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18713869
http://purl.uniprot.org/uniprot/P53218#attribution-E051AE176AF017BB56A121A74CD8D98Ahttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18713869
http://purl.uniprot.org/uniprot/P41812#attribution-E051AE176AF017BB56A121A74CD8D98Ahttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18713869
http://purl.uniprot.org/uniprot/P38786#attribution-E051AE176AF017BB56A121A74CD8D98Ahttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18713869
http://purl.uniprot.org/uniprot/P40571#attribution-E051AE176AF017BB56A121A74CD8D98Ahttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18713869
http://purl.uniprot.org/uniprot/#_P41812-mappedCitation-18713869http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18713869