Footprinting analysis demonstrates extensive similarity between eukaryotic RNase P and RNase MRP holoenzymes

RNA. 2008 Aug;14(8):1558-67. doi: 10.1261/rna.1106408. Epub 2008 Jun 25.

Abstract

Eukaryotic ribonuclease (RNase) P and RNase MRP are evolutionary related RNA-based enzymes involved in metabolism of various RNA molecules, including tRNA and rRNA. In contrast to the closely related eubacterial RNase P, which is comprised of an RNA component and a single small protein, these enzymes contain multiple protein components. Here we report the results of footprinting studies performed on purified Saccharomyces cerevisiae RNase MRP and RNase P holoenzymes. The results identify regions of the RNA components affected by the protein moiety, suggest a role of the proteins in stabilization of the RNA fold, and point to substantial similarities between the two evolutionary related RNA-based enzymes.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Endoribonucleases / chemistry*
  • Endoribonucleases / metabolism
  • Evolution, Molecular
  • Molecular Sequence Data
  • Protein Footprinting
  • RNA, Catalytic / chemistry
  • RNA, Catalytic / metabolism*
  • RNA, Fungal / chemistry
  • RNA, Fungal / metabolism*
  • Ribonuclease P / chemistry*
  • Ribonuclease P / metabolism
  • Ribonucleoproteins / chemistry*
  • Ribonucleoproteins / metabolism
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / metabolism

Substances

  • RNA, Catalytic
  • RNA, Fungal
  • Ribonucleoproteins
  • Saccharomyces cerevisiae Proteins
  • Endoribonucleases
  • mitochondrial RNA-processing endoribonuclease
  • Ribonuclease P