Metal ion and substrate structure dependence of the processing of tRNA precursors by RNase P and M1 RNA

Christopher K. Surrattt, Barbara J. Carter, Robert C. Payne, Sidney M. Hecht

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19 Scopus citations


A synthetic tRNA precursor analog containing the structural elements of Escherichia coli tRNAPhe was characterized as a substrate for E. coli ribonuclease P and for M1 RNA, the catalytic RNA subunit. Processing of the synthetic precursor exhibited a Mg2+ dependence quite similar to that of natural tRNA precursors such as E. coli tRNATyr precursor. It was found that Sr2+, Ca2+, and Ba2+ ions promoted processing of the dimeric precursor at Mg2+ concentrations otherwise insufficient to support processing; very similar behavior was noted for E. coli tRNATyr. As noted previously for natural tRNA precursors, the absence of the 3′-terminal CA sequence in the synthetic precursor diminished the facility of processing of this substrate by RNase P and M1 RNA. A study of the Mg2+ dependence of processing of the synthetic tRNA dimeric substrate radiolabeled between C75 and A76 provided unequivocal evidence for an alteration in the actual site of processing by E. coli RNase P as a function of Mg2+ concentration. This property was subsequently demonstrated to obtain (Carter, B. J., Vold, B. S., and Hecht, S. M. (1990) J. Biol. Chem. 265, 7100-7103) for a mutant Bacillus subtilis tRNAHis precursor containing a potential A-C base pair at the end of the acceptor stem.

Original languageEnglish (US)
Pages (from-to)22513-22519
Number of pages7
JournalJournal of Biological Chemistry
Issue number36
StatePublished - Dec 25 1990
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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