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

  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},

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Structure in solution of M1 RNA, the catalytic subunit of ribonuclease P from Escherichia coli.

The structure of M1 RNA, the RNA component of Escherichia coli RNase P, has been probed by mild digestion with a variety of ribonucleases. The results have been used to generate a model for the

Metal ion requirements and other aspects of the reaction catalyzed by M1 RNA, the RNA subunit of ribonuclease P from Escherichia coli.

Many aspects of the reaction catalyzed by M1 RNA are compatible with a mechanism in which phosphodiester bond cleavage is mediated by metal ion.

Interaction of the Bacillus subtilis RNase P with the 30S ribosomal subunit.

The results suggest that the dimeric form of the RNase P is primarily involved in 30S ribosome binding, and Hydroxyl radical protection and chemical modification identify several protected residues located in a highly conserved region in theRNase P RNA.

Chloroplast ribonuclease P does not utilize the ribozyme-type pre-tRNA cleavage mechanism.

Partially purified RNase P from spinach chloroplasts can accurately and efficiently process phosphorothioate-substituted pre-tRNAs; cleavage occurs exclusively at the thio-containing scissile bond, consistent with a general chemical effect of the phosphate substitution rather than with a metal coordination deficiency.

Specific interactions in RNA enzyme-substrate complexes.

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.

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.

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

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.



Ribonuclease P: an enzyme with an essential RNA component.

The activity of ribonuclease P on precursor tRNA substrates from Escherichia coli can be abolished by pretreatment of this enzyme with micrococcal nuclease or pancreatic ribonuclease A, as well as by

RNase P of Bacillus subtilis has a RNA component.

Purification and properties of a specific Escherichia coli ribonuclease which cleaves a tyrosine transfer ribonucleic acid presursor.

In the course of purifying RNase P, it is discovered in other subcellular fractions of E. coli RNase activities potentially responsible for additional steps of precursor tRNA processing.

Properties of purified ribonuclease P from Escherichia coli.

The purified protein moiety of ribonuclease P (EC from Escherichia coli, a single polypeptide of molecular weight approximately 17 500, has not catalytic activity by itself on several RNA

E. coli RNAase P has a required RNA component in vivo

Partial purification of RNase P from Schizosaccharomyces pombe.

Precursor molecules of Escherichia coli transfer RNAs accumulated in a temperature-sensitive mutant.

Nucleotide sequence and in vitro processing of a precursor molecule to Escherichia coli 4.5 S RNA.