ArticleProceedings of the National Academy of Sciences of the United States of America2002
A protein subunit of human RNase P, Rpp14, and its interacting partner, OIP2, have 3'-->5' exoribonuclease activity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- RNase P: Beyond Precursor tRNA Processing.Genomics, proteomics & bioinformatics · 2024Review
- Human RNase P exhibits and controls distinct ribonucleolytic activities required for ordered maturation of tRNA.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Dynamic Network of RNP RNase P Subunits.International journal of molecular sciences · 2021Review
- Learning-induced mRNA alterations in olfactory bulb mitral cells in neonatal rats.Learning & memory (Cold Spring Harbor, N.Y.) · 2020Article
- Chance and necessity in the evolution of RNase P.RNA (New York, N.Y.) · 2018Article
- Ribonuclease P.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2011Article
- RNA binding properties of conserved protein subunits of human RNase P.Nucleic acids research · 2011Article
- Of proteins and RNA: the RNase P/MRP family.RNA (New York, N.Y.) · 2010Review
- MPP6 is an exosome-associated RNA-binding protein involved in 5.8S rRNA maturation.Nucleic acids research · 2005Article
- Coordinate inhibition of expression of several genes for protein subunits of human nuclear RNase P.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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.
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