Alterations in the intracellular level of a protein subunit of human RNase P affect processing of tRNA precursors

Amit Cohen, Robert Reiner, Nayef Jarrous*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

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.

Original languageAmerican English
Pages (from-to)4836-4846
Number of pages11
JournalNucleic Acids Research
Volume31
Issue number16
DOIs
StatePublished - 15 Aug 2003

Bibliographical note

Funding Information:
Part of this study was initiated in the laboratory of Professor Sidney Altman at Yale University. This research was supported by the Israel Science Foundation (grant no. 549/ 01) and by the United States–Israel Binational Science Foundation (grant no. 2001017) to N.J. N.J. is the recipient of a Kahanoff Foundation fellowship.

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