The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme

Cecilia Guerrier-Takada, Katheleen Gardiner, Terry Marsh, Norman Pace, Sidney Altman

Research output: Contribution to journalArticle

1848 Scopus citations

Abstract

The RNA moieties of ribonuclease P purified from both E. coli (M1 RNA) and B. subtilis (P-RNA) can cleave tRNA precursor molecules in buffers containing either 60 mM Mg2+ or 10 mM Mg2+ plus 1 mM spermidine. The RNA acts as a true catalyst under these conditions whereas the protein moieties of the enzymes alone show no catalytic activity. However, in buffers containing 5-10 mM Mg2+ (in the absence of spermidine) both kinds of subunits are required for enzymatic activity, as shown previously. In the presence of low concentrations of Mg2+, in vitro, the RNA and protein subunits from one species can complement subunits from the other species in reconstitution experiments. When the precursor to E. coli 4.5S RNA is used as a substrate, only the enzyme complexes formed with M1 RNA from E. coli and the protein moieties from either bacterial species are active.

Original languageEnglish (US)
Pages (from-to)849-857
Number of pages9
JournalCell
Volume35
Issue number3 PART 2
DOIs
StatePublished - Dec 1983
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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    Guerrier-Takada, C., Gardiner, K., Marsh, T., Pace, N., & Altman, S. (1983). The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme. Cell, 35(3 PART 2), 849-857. https://doi.org/10.1016/0092-8674(83)90117-4