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. 1983 Dec;35(3 Pt 2):849-57.
doi: 10.1016/0092-8674(83)90117-4.

The RNA Moiety of Ribonuclease P Is the Catalytic Subunit of the Enzyme

The RNA Moiety of Ribonuclease P Is the Catalytic Subunit of the Enzyme

C Guerrier-Takada et al. Cell. .

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.

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