Human RNase P exhibits and controls distinct ribonucleolytic activities required for ordered maturation of tRNA

Natalie Orlovetskie, Dhivakar Mani, Alexander Rouvinski, Nayef Jarrous*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

Precursor tRNAs are transcribed with flanking and intervening sequences known to be processed by specific ribonucleases. Here, we show that transcription complexes of RNA polymerase III assembled on tRNA genes comprise RNase P that cleaves precursor tRNA and subsequently degrades the excised 5′ leader. Degradation is based on a 3′–5′ exoribonucleolytic activity carried out by the protein subunit Rpp14, as determined by biochemical and reverse genetic analyses. Neither reconstituted nor purified RNase P displays this magnesium ion-dependent, processive exoribonucleolytic activity. Markedly, knockdown of Rpp14 by RNA interference leads to a wide-ranging inhibition of cleavage of flanking and intervening sequences of various precursor tRNAs in extracts and cells. This study reveals that RNase P controls tRNA splicing complex and RNase Z for ordered maturation of nascent precursor tRNAs by transcription complexes.

Original languageAmerican English
Article numbere2307185120
JournalProceedings of the National Academy of Sciences of the United States of America
Volume120
Issue number42
DOIs
StatePublished - 17 Oct 2023

Bibliographical note

Publisher Copyright:
Copyright © 2023 the Author(s).

Keywords

  • RNA polymerase III
  • RNase P
  • exoribonuclease
  • tRNA
  • transcription complex

Fingerprint

Dive into the research topics of 'Human RNase P exhibits and controls distinct ribonucleolytic activities required for ordered maturation of tRNA'. Together they form a unique fingerprint.

Cite this