Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA

Yanglong Zhu, Vilius Stribinskis, Kenneth S. Ramos, Yong Li

Research output: Contribution to journalArticle

19 Scopus citations

Abstract

RNase MRP is a eukaryote-specific endoribonuclease that generates RNA primers for mitochondrial DNA replication and processes precursor rRNA. RNase P is a ubiquitous endoribonuclease that cleaves precursor tRNA transcripts to produce their mature 5′ termini. We found extensive sequence homology of catalytic domains and specificity domains between their RNA subunits in many organisms. In Candida glabrata, the internal loop of helix P3 is 100% conserved between MRP and P RNAs. The helix P8 of MRP RNA from microsporidia Encephalitozoon cuniculi is identical to that of P RNA. Sequence homology can be widely spread over the whole molecule of MRP RNA and P RNA, such as those from Dictyostelium discoideum. These conserved nucleotides between the MRP and P RNAs strongly support the hypothesis that the MRP RNA is derived from the P RNA molecule in early eukaryote evolution.

Original languageEnglish (US)
Pages (from-to)699-706
Number of pages8
JournalRNA
Volume12
Issue number5
DOIs
StatePublished - May 1 2006
Externally publishedYes

Keywords

  • Catalytic domain
  • RNase MRP RNA
  • Specificity domain

ASJC Scopus subject areas

  • Molecular Biology

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