Two helices plus a linker: a small model substrate for eukaryotic RNase P

Proc Natl Acad Sci U S A. 1995 Mar 28;92(7):2627-31. doi: 10.1073/pnas.92.7.2627.

Abstract

Using precursor tRNA molecules to study RNA-protein interactions, we have identified an RNA motif recognized by eukaryotic RNase P (EC 3.1.26.5). Analysis of circularly permuted precursors indicates that interruptions in the sugar-phosphate backbone are not tolerated in the acceptor stem, in the T stem-loop, or between residues A-9 and G-10. Prokaryotic RNase P will function with a minihelix consisting of the acceptor stem connected directly to the T stem-loop. Eukaryotic RNase P cannot use such a minimal substrate unless a linker sequence is added in the gap where the D stem and anticodon stem-loop were deleted.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • DNA-Directed RNA Polymerases / metabolism
  • Endoribonucleases / metabolism*
  • Kinetics
  • Models, Structural
  • Molecular Sequence Data
  • Mutagenesis
  • Nucleic Acid Conformation*
  • RNA Precursors / chemistry*
  • RNA Precursors / metabolism*
  • RNA, Catalytic / metabolism*
  • RNA, Transfer, Phe / chemistry*
  • RNA, Transfer, Phe / metabolism*
  • Ribonuclease P
  • Substrate Specificity
  • Templates, Genetic
  • Transcription, Genetic
  • Viral Proteins
  • Xenopus laevis

Substances

  • RNA Precursors
  • RNA, Catalytic
  • RNA, Transfer, Phe
  • Viral Proteins
  • bacteriophage T7 RNA polymerase
  • DNA-Directed RNA Polymerases
  • Endoribonucleases
  • Ribonuclease P