Genetic and biochemical analyses of yeast RNase MRP

David Tollervey*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

RNase MRP cleaves the yeast pre-rRNA at a site in internal transcribed spacer 1 (ITS1) and this cleavage can be reproduced in vitro by the highly purified enzyme. Two protein components (Pop1p and Pop2p) have been identified which are common to yeast RNase MRP and RNase P. Moreover, purified RNase P can also cleave the pre-rRNA substrate in vitro, underlining the similarities between these particles. Genetic evidence suggests that RNase MRP functionally interacts with the snoRNPs which are required for other pre-rRNA processing reactions.

Original languageEnglish
Pages (from-to)75-79
Number of pages5
JournalMolecular Biology Reports: An International Journal on Molecular and Cellular Biology
Volume22
Issue number2
DOIs
Publication statusPublished - Jun 1995

Keywords

  • ribosome synthesis
  • RNA processing
  • RNase MRP
  • rRNA
  • saccharomyces cerevisiae
  • snoRNA

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