The POP1 gene encodes a protein component common to the RNase MRP and RNase P ribonucleoproteins

Zoi Lygerou*, Philip Mitchell, Elisabeth Petfalski, Bertrand Séraphin, David Tollervey

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Two forms of the yeast 5.8S rRNA are generated from a large precursor by distinct processing pathways. Cleavage at site A3 is required for synthesis of the major, short form, designated 5.8S(S), but not for synthesis of the long form, 5.8S(L). To identify components required for A3 cleavage, a bank of temperature-sensitive lethal mutants was screened for those with a reduced ratio of 5.8S(S); 5.8S(L). The pop1-1 mutation (for processing of precursor RNAs) shows this phenotype and also inhibits A3 cleavage. The pre-rRNA processing defect of pop1-1 strains is similar to that reported for mutations in the RNA component of RNase MRP; we show that a mutation in the RNase MRP RNA also inhibits cleavage at site A3. This is the first site shown to require RNase MRP for cleavage in vivo. The pop1-1 mutation also leads to a block in the processing of pre-tRNA that is identical to that reported for mutations in the RNA component of RNase P. The RNA components of both RNase MRP and RNase P are underaccumulated in pop1-1 strains at the nonpermissive temperature, and immunoprecipitation demonstrates that POP1p is a component of both ribonucleoproteins. The POP1 gene encodes a protein with a predicted molecular mass of 100.5 kD and is essential for viability. POP1p is the first protein component of the nuclear RNase P or RNase MRP for which the gene has been cloned.

Original languageEnglish
Pages (from-to)1423-1433
Number of pages11
JournalGenes and Development
Volume8
Issue number12
DOIs
Publication statusPublished - 15 Jun 1994

Keywords

  • POP1 gene
  • RNA processing
  • RNase MRP
  • RNase P
  • S. cerevisiae

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