Abstract
The gene for an essential protein subunit of nuclear RNase P from Saccharomyces cerevisiae has been cloned. The gene for this protein, RPP1, was identified by virtue of its homology with a human scleroderma autoimmune antigen, Rpp30, which copurifies with human RNase P. Epitope-tagged Rpp1 can be found in association with both RNase P RNA and a related endoribonuclease, RNase MRP RNA, in immunoprecipitates from crude extracts of cells. Depletion of Rpp1 in vivo leads to the accumulation of precursor tRNAs with unprocessed 5' and 3' termini and reveals rRNA processing defects that have not been described previously for proteins associated with RNase P or RNase MRP. Immunoprecipitated complexes cleave both yeast precursor tRNAs and precursor rRNAs.
Publication types
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Research Support, U.S. Gov't, P.H.S.
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Corrected and Republished Article
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Cloning, Molecular
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Endoribonucleases / chemistry
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Endoribonucleases / genetics
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Endoribonucleases / metabolism*
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Genes, Fungal*
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Humans
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Macromolecular Substances
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Molecular Sequence Data
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RNA Precursors / metabolism*
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RNA, Catalytic / genetics
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RNA, Catalytic / metabolism*
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RNA, Fungal / metabolism
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RNA, Ribosomal / biosynthesis*
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RNA, Transfer / biosynthesis
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Ribonuclease P
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Saccharomyces cerevisiae / genetics*
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins*
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Sequence Alignment
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Sequence Homology, Amino Acid
Substances
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Macromolecular Substances
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RNA Precursors
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RNA, Catalytic
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RNA, Fungal
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RNA, Ribosomal
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Saccharomyces cerevisiae Proteins
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RNA, Transfer
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Endoribonucleases
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RPP1 protein, S cerevisiae
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RPP14 protein, human
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Ribonuclease P