Abstract
The processing of precursor tRNAs at their 5' and 3' termini is a fundamental event in the biosynthesis of tRNA. RNase P is generally responsible for endonucleolytic removal of a leader sequence of precursor tRNA to generate the mature 5' terminus. However, much less is known about the RNase P counterparts or other proteins that are active at the tRNA 3' terminus. Here we show that one of the human RNase P subunits, Rpp14, together with one of its interacting protein partners, OIP2, is a 3'-->5' exoribonuclease with a phosphorolytic activity that processes the 3' terminus of precursor tRNA. Immunoprecipitates of a crude human RNase P complex can process both ends of precursor tRNA by hydrolysis, but purified RNase P has no exonuclease activity. Rpp14 and OIP2 may be part of an exosome activity.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Carrier Proteins / chemistry*
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Chromatography, Thin Layer
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DNA / chemistry
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Endoribonucleases / chemistry*
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Endoribonucleases / metabolism
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Escherichia coli / metabolism
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Escherichia coli Proteins*
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Exoribonucleases / chemistry
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Exosome Multienzyme Ribonuclease Complex
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HeLa Cells
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Humans
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Hydrolysis
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Phosphorylation
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Precipitin Tests
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Protein Binding
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Protein Structure, Tertiary
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RNA, Catalytic / chemistry*
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RNA, Catalytic / metabolism
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RNA, Transfer / chemistry*
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RNA, Transfer, Tyr / chemistry
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RNA-Binding Proteins
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Ribonuclease P
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Time Factors
Substances
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Carrier Proteins
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Escherichia coli Proteins
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RNA, Catalytic
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RNA, Transfer, Tyr
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RNA-Binding Proteins
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Recombinant Proteins
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DNA
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RNA, Transfer
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EXOSC8 protein, human
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Endoribonucleases
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Exoribonucleases
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Exosome Multienzyme Ribonuclease Complex
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RPP14 protein, human
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Ribonuclease P
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ribonuclease P, E coli