Kinetics of the processing of the precursor to 4·5 S RNA, a naturally occurring substrate for RNase P from Escherichia coli

Karen A. Peck-Miller, Sidney Altman

Research output: Contribution to journalArticle

122 Scopus citations

Abstract

A study was made of the cleavage by M1 RNA and RNase P of a non-tRNA precursor that can serve as a substrate for RNase P from Escherichia coli, namely, the precursor to 4·5 S RNA (p4·5S). The overall efficiency of cleavage of p4·5S by RNase P is similar to that of wild-type tRNA precursors. However, unlike the reaction with wild-type tRNA precursors, the reaction catalyzed by the holoenzyme with p4·5S as substrate has a much lower Km value than that catalyzed by M1 RNA with the same substrate, indicating that the protein subunit plays a crucial role in the recognition of p4·5S. A model hairpin substrate, based on the sequence of p4·5S, is cleaved with greater efficiency that the parent molecule. The 3′-terminal CCC sequence of p4·5 S may be as important for cleavage of this substrate as the 3′-terminal CCA sequence is for cleavage of tRNA precursors.

Original languageEnglish (US)
Pages (from-to)1-5
Number of pages5
JournalJournal of molecular biology
Volume221
Issue number1
DOIs
StatePublished - Sep 5 1991
Externally publishedYes

Keywords

  • 4·5 S RNA precursor
  • M1 RNA
  • RNase P
  • enzyme kinetics

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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