Model substrates for an RNA enzyme

Science. 1987 Oct 23;238(4826):527-30. doi: 10.1126/science.2443980.

Abstract

M1 RNA, the catalytic RNA subunit of Escherichia coli ribonuclease P, can cleave novel transfer RNA (tRNA) precursors that lack specific domains of the normal tRNA sequence. The smallest tRNA precursor that was cleaved efficiently retained only the domain of the amino acid acceptor stem and the T stem and loop. The importance of the 3' terminal CCA nucleotide residues in the processing of both novel and normal tRNA precursors implies that the same enzymatic function of M1 RNA is involved.

Publication types

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

MeSH terms

  • Base Sequence
  • DNA / genetics
  • DNA, Recombinant
  • Endoribonucleases / metabolism*
  • Escherichia coli / enzymology*
  • Escherichia coli Proteins*
  • Molecular Sequence Data
  • Mutation
  • Nucleic Acid Conformation
  • Plasmids
  • RNA Precursors / metabolism*
  • RNA, Bacterial / genetics
  • RNA, Transfer, Amino Acyl / genetics
  • Ribonuclease P
  • Ribonuclease T1 / metabolism
  • Structure-Activity Relationship
  • Substrate Specificity
  • Suppression, Genetic

Substances

  • DNA, Recombinant
  • Escherichia coli Proteins
  • RNA Precursors
  • RNA, Bacterial
  • RNA, Transfer, Amino Acyl
  • DNA
  • Endoribonucleases
  • Ribonuclease P
  • ribonuclease P, E coli
  • Ribonuclease T1