Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2000-1-27
pubmed:abstractText
The exosome is a protein complex consisting of a variety of 3'-to-5' exonucleases that functions both in 3'-to-5' trimming of rRNA precursors and in 3'-to-5' degradation of mRNA. To determine additional exosome functions, we examined the processing of a variety of RNAs, including tRNAs, small nuclear RNAs (snRNAs), small nucleolar RNAs (snoRNAs), RNase P, RNase MRP, and SRP RNAs, and 5S rRNAs in mutants defective in either the core components of the exosome or in other proteins required for exosome function. These experiments led to three important conclusions. First, exosome mutants accumulate 3'-extended forms of the U4 snRNA and a wide variety of snoRNAs, including snoRNAs that are independently transcribed or intron derived. This finding suggests that the exosome functions in the 3' end processing of these species. Second, in exosome mutants, transcripts for U4 snRNA and independently transcribed snoRNAs accumulate as 3'-extended polyadenylated species, suggesting that the exosome is required to process these 3'-extended transcripts. Third, processing of 5.8S rRNA, snRNA, and snoRNA by the exosome is affected by mutations of the nuclear proteins Rrp6p and Mtr4p, whereas mRNA degradation by the exosome required Ski2p and was not affected by mutations in RRP6 or MTR4. This finding suggests that the cytoplasmic and nuclear forms of the exosome represent two functionally different complexes involved in distinct 3'-to-5' processing and degradation reactions.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-10465791, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-10508172, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-1620131, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-2247609, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-2659436, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-321129, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-3534883, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-6251092, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-7574504, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-7626803, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-7739552, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-7891709, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-8045930, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-8052314, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-8393418, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-8534909, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-8600032, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-8720068, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-8756671, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-8816497, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-8982072, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-9159079, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-9334335, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-9390555, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-9409624, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-9463390, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-9482746, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-9488433, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-9582370, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-9584178, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-9649442, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-9705492, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-9770456, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-9774670, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-9837720, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-9889288, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-9891049, http://linkedlifedata.com/resource/pubmed/commentcorrection/10611222-9891085
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/DEAD-box RNA Helicases, http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Exoribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/MTR4 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Poly A, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Fungal, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Nuclear, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Nucleolar, http://linkedlifedata.com/resource/pubmed/chemical/RNA Helicases, http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNT1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/RRP6 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease III, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0270-7306
pubmed:author
pubmed:issnType
Print
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
441-52
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10611222-Mutation, pubmed-meshheading:10611222-Fungal Proteins, pubmed-meshheading:10611222-Saccharomyces cerevisiae, pubmed-meshheading:10611222-Kinetics, pubmed-meshheading:10611222-Genes, pubmed-meshheading:10611222-Saccharomyces cerevisiae Proteins, pubmed-meshheading:10611222-RNA, Messenger, pubmed-meshheading:10611222-Phenotype, pubmed-meshheading:10611222-Transcription, Genetic, pubmed-meshheading:10611222-Endoribonucleases, pubmed-meshheading:10611222-Exoribonucleases, pubmed-meshheading:10611222-RNA, Fungal, pubmed-meshheading:10611222-Poly A, pubmed-meshheading:10611222-Multienzyme Complexes, pubmed-meshheading:10611222-Genes, Fungal, pubmed-meshheading:10611222-Ribonuclease III, pubmed-meshheading:10611222-RNA Processing, Post-Transcriptional, pubmed-meshheading:10611222-RNA, Small Nuclear, pubmed-meshheading:10611222-RNA-Binding Proteins
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