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

@article{GuerrierTakada1983TheRM,
  title={The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme},
  author={Cecilia Guerrier-Takada and Katheleen J. Gardiner and Terry L. Marsh and Norman R. Pace and Sidney Altman},
  journal={Cell},
  year={1983},
  volume={35},
  pages={849-857}
}

Figures from this paper

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Specific interactions in RNA enzyme-substrate complexes.

TLDR
The data demonstrate that in RNA's with very different cellular functions, there are domains with similar structural and functional properties and that there is a nucleotide in M1 RNA that affects the site of cleavage by the enzyme.

Catalytic activity of an RNA molecule prepared by transcription in vitro.

TLDR
The RNA moiety M1RNA of ribonuclease P from Escherichia coli and the unprocessed transcript prepared in vitro of the gene for M1 RNA can both perform the cleavage reactions of the canonical enzyme in the absence of the protein moiety.

Importance of RNA-protein interactions in bacterial ribonuclease P structure and catalysis.

TLDR
The role of RNA-protein interactions in bacterial RNase P is examined from both structural and mechanistic perspectives to serve a number of critical roles in the RNP including stabilizing the structure, and enhancing the affinity for substrates and metal ions.

Escherichia coli ribonuclease P.

Structural Studies of Ribonuclease P

TLDR
Structures of the specificity domain and of the entire RNA component of RNase P from two different bacteria have been described and provide the first atomic level information on the structure of the RNA component, contributing to an atomic level understanding of the architecture ofRNase P.
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