Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2000-4-27
pubmed:abstractText
The biogenesis of a number of RNA species in eukaryotic cells requires 3' processing. To determine the enzymes responsible for these trimming events, we created yeast strains lacking specific 3' to 5' exonucleases. In this work, we describe the analysis of three members of the RNase D family of exonucleases (Rex1p, Rex2p and Rex3p). This work led to three important conclusions. First, each of these exonucleases is required for the processing of distinct RNAs. Specifically, Rex1p, Rex2p and Rex3p are required for 5S rRNA, U4 snRNA and MRP RNA trimming, respectively. Secondly, some 3' exonucleases are redundant with other exonucleases. Specifically, Rex1p and Rex2p function redundantly in 5.8S rRNA maturation, Rex1p, Rex2p and Rex3p are redundant for the processing of U5 snRNA and RNase P RNA, and Rex1p and the exonuclease Rrp6p have an unknown redundant essential function. Thirdly, the demonstration that the Rex proteins can affect reactions that have been attributed previously to the exosome complex indicates that an apparently simple processing step can be surprisingly complex with multiple exonucleases working sequentially in the same pathway.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-10359084, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-10465791, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-10508172, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-10567561, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-10571176, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-11894949, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-1990278, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-2666158, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-2981839, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-6253814, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-7854324, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-8550599, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-8600032, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-8816497, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-9150139, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-9235947, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-9334335, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-9390555, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-9396823, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-9443958, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-9482746, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-9569007, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-9582370, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-9736620, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-9774670, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716935-9933355
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Catalytic, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Fungal, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal, 5.8S, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal, 5S, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Nuclear, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Arg, http://linkedlifedata.com/resource/pubmed/chemical/RNT1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease III, http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease P, http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/mitochondrial RNA-processing...
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1357-65
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:10716935-Conserved Sequence, pubmed-meshheading:10716935-Endoribonucleases, pubmed-meshheading:10716935-Gene Deletion, pubmed-meshheading:10716935-Genes, Fungal, pubmed-meshheading:10716935-RNA, Catalytic, pubmed-meshheading:10716935-RNA, Fungal, pubmed-meshheading:10716935-RNA, Ribosomal, pubmed-meshheading:10716935-RNA, Ribosomal, 5.8S, pubmed-meshheading:10716935-RNA, Ribosomal, 5S, pubmed-meshheading:10716935-RNA, Small Nuclear, pubmed-meshheading:10716935-RNA, Transfer, Arg, pubmed-meshheading:10716935-RNA Processing, Post-Transcriptional, pubmed-meshheading:10716935-RNA Stability, pubmed-meshheading:10716935-Ribonuclease III, pubmed-meshheading:10716935-Ribonuclease P, pubmed-meshheading:10716935-Ribonucleases, pubmed-meshheading:10716935-Saccharomyces cerevisiae, pubmed-meshheading:10716935-Saccharomyces cerevisiae Proteins, pubmed-meshheading:10716935-Substrate Specificity
pubmed:year
2000
pubmed:articleTitle
Three conserved members of the RNase D family have unique and overlapping functions in the processing of 5S, 5.8S, U4, U5, RNase MRP and RNase P RNAs in yeast.
pubmed:affiliation
Department of Molecular Biology, Howard Hughes Medical Institute, University of Arizona, Tucson, AZ 85721, USA. ambro@u.arizona.edu
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't