ArticleNucleic acids research2003
Alterations in the intracellular level of a protein subunit of human RNase P affect processing of tRNA precursors.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- VIRMA-mediated mScience advances · 2025Article
- Both endonucleolytic and exonucleolytic cleavage mediate ITS1 removal during human ribosomal RNA processing.The Journal of cell biology · 2013Article
- Unexpected diversity of RNase P, an ancient tRNA processing enzyme: challenges and prospects.FEBS letters · 2010Review
- Heterodimerization regulates RNase MRP/RNase P association, localization, and expression of Rpp20 and Rpp25.RNA (New York, N.Y.) · 2007Article
- A role for the catalytic ribonucleoprotein RNase P in RNA polymerase III transcription.Genes & development · 2006Article
- MPP6 is an exosome-associated RNA-binding protein involved in 5.8S rRNA maturation.Nucleic acids research · 2005Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
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Abstract
The human ribonucleoprotein ribonuclease P (RNase P), processing tRNA, has at least 10 distinct protein subunits. Many of these subunits, including the autoimmune antigen Rpp38, are shared by RNase MRP, a ribonucleoprotein enzyme required for processing of rRNA. We here show that constitutive expression of exogenous, tagged Rpp38 protein in HeLa cells affects processing of tRNA precursors. Alterations in the site-specific cleavage and in the steady-state level of 3' sequences of the internal transcribed spacer 1 of rRNA are also observed. These processing defects are accompanied by selective shut-off of expression of Rpp38 and by low expression of the tagged protein. RNase P purified from these cells exhibits impaired activity in vitro. Moreover, inhibition of Rpp38 by the use of small interfering RNA causes accumulation of the initiator methionine tRNA precursor. Expression of other protein components, but not of the H1 RNA subunit, is coordinately inhibited. Our results reveal that normal expression of Rpp38 is required for the biosynthesis of intact RNase P and for the normal processing of stable RNA in human cells.
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