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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
21
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pubmed:dateCreated |
1998-6-25
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pubmed:databankReference | |
pubmed:abstractText |
The eukaryotic 25 S, 18 S, and 5.8 S rRNAs are synthesized as a single transcript with two internal transcribed spacers (ITS1 and ITS2), which are removed by endo- and exoribonucleolytic steps to produce mature rRNA. Genetic selection for suppressors of a polyadenylation defect yielded two cold-sensitive alleles of a gene that we named RRP6 (ribosomal RNA processing). Molecular cloning of RRP6 revealed its homology to a 100-kDa human, nucleolar PM-Scl autoantigen and to Escherichia coli RNase D, a 3'-5' exoribonuclease. Recessive mutations in rrp6 result in the accumulation of a novel 5. 8 S rRNA processing intermediate, called 5.8 S*, which has normal 5' ends, but retains approximately 30 nucleotides of ITS2. Pulse-chase analysis of 5.8 S rRNA processing in an rrp6- strain revealed a precursor-product relationship between 5.8 S* and 5.8 S rRNAs, suggesting that Rrp6p plays a role in the removal of the last 30 nucleotides of ITS2 from 5.8 S precursors. A portion of 5.8 S* rRNA assembles into 60 S ribosomes which form polyribosomes, suggesting that they function in protein synthesis. These findings indicate that Rrp6p plays a role in 5.8 S rRNA 3' end formation, and they identify a functional intermediate in the rRNA processing pathway.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Autoantigens,
http://linkedlifedata.com/resource/pubmed/chemical/Exoribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal, 5.8S,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/polymyosistis-scleroderma antigen...
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
13255-63
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9582370-Amino Acid Sequence,
pubmed-meshheading:9582370-Autoantigens,
pubmed-meshheading:9582370-Cloning, Molecular,
pubmed-meshheading:9582370-Exoribonucleases,
pubmed-meshheading:9582370-Fungal Proteins,
pubmed-meshheading:9582370-Genes, Suppressor,
pubmed-meshheading:9582370-Humans,
pubmed-meshheading:9582370-Molecular Sequence Data,
pubmed-meshheading:9582370-Mutation,
pubmed-meshheading:9582370-Open Reading Frames,
pubmed-meshheading:9582370-RNA, Ribosomal, 5.8S,
pubmed-meshheading:9582370-RNA Processing, Post-Transcriptional,
pubmed-meshheading:9582370-Saccharomyces cerevisiae,
pubmed-meshheading:9582370-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:9582370-Sequence Homology, Amino Acid
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pubmed:year |
1998
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pubmed:articleTitle |
Rrp6p, the yeast homologue of the human PM-Scl 100-kDa autoantigen, is essential for efficient 5.8 S rRNA 3' end formation.
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pubmed:affiliation |
Department of Microbiology and Immunology, University of Rochester School of Medicine and Dentistry, Rochester, New York 14618, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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