Enhancement of RNA annealing and strand displacement found in archaeal ribonuclease P proteins is conserved in Escherichia coli protein C5 and yeast protein Rpr2

Biosci Biotechnol Biochem. 2014;78(10):1700-2. doi: 10.1080/09168451.2014.925780. Epub 2014 Jun 26.

Abstract

We analyzed modes of action of ribonuclease P (RNase P) proteins, C5 in Escherichia coli and Rpr2 in Saccharomyces cerevisiae, using a pair of complementary fluorescence-labeled oligoribonucleotides. Fluorescence resonance energy transfer-based assays revealed that RNA annealing and strand displacement activities found in archaeal RNase P proteins are prevalent in eubacterial (C5) and eukaryotic (Rpr2) RNase P proteins.

Keywords: Pyrococcus horikoshii; RNA chaperone; RNA-binding protein; RNase P proteins; fluorescence resonance energy transfer.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Escherichia coli Proteins / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Pyrococcus horikoshii / enzymology*
  • RNA / metabolism*
  • Ribonuclease P / chemistry
  • Ribonuclease P / metabolism*
  • Saccharomyces cerevisiae Proteins / metabolism*

Substances

  • Escherichia coli Proteins
  • Saccharomyces cerevisiae Proteins
  • RNA
  • Ribonuclease P
  • Rpr2 protein, S cerevisiae
  • ribonuclease P, E coli