Enzymatic cleavage of RNA by RNA

  title={Enzymatic cleavage of RNA by RNA},
  author={Sidney Altman},
  journal={Bioscience Reports},
  • S. Altman
  • Published 1 December 1986
  • Biology
  • Bioscience Reports
The discovery and characterization of the catalytic RNA subunit of the enzyme ribonuclease P ofEscherichia coli is described. 

Distal to Proximal—Functional Coupling in RNase P RNA-mediated Catalysis

Bacterial RNase P contains one RNA (RPR) and one protein (RPP) subunit, however, the number of protein subunits is small.

The varieties of ribonuclease P.

Structure and Function of Bacterial RNase P

RNase P is an endoribonuclease that cleaves tRNA precursors to generate the 5′-ends of mature tRNAs in prokaryotes and the reaction of the RNA with its substrates follows Michaelis-Menten kinetics.

Ribonuclease P as a snRNP

In the absence of direct cloning of the gene for the RNA component and functional assays of the transcript of that cloned gene, it is possible to perform other biochemical tests to determine if the enzymatic activity has an essential RNA component.

Structural and functional similarities between MRP and RNase P

RNase P, the enzyme responsible for 5′-end processing of tRNAs and 4.5S RNA, has been extensively characterized from E. coli and is the first true RNA enzyme to be characterized.

Ribozymes: catalytic RNAs that cut things, make things, and do odd and useful jobs.

Catalytic RNAs, or ribozymes, are a fossil record of the ancient molecular evolution of life on earth and still provide the essential core of macromolecule synthesis in all life forms today. Are they



Identification of tRNA precursor molecules made by phage T4.

Precursors to the bacteriophage T4 tRNAs consist of polynucleotide chains containing two tRNA species

The chemistry of self-splicing RNA and RNA enzymes.

  • T. Cech
  • Biology, Chemistry
  • 1987
The chemical mechanisms of RNA-catalyzed reactions are discussed with emphasis on the self-splicing ribosomal RNA precursor of Tetrahymena and the enzymatic activities of its intervening sequence RNA.

Model substrates for an RNA enzyme.

The importance of the 3' terminal CCA nucleotide residues in the processing of both novel and normal tRNA precursors implies that the same enzymatic function of M1 RNA is involved.

Role of the protein moiety of ribonuclease P, a ribonucleoprotein enzyme.

Kinetic analyses show that high salt concentrations facilitate substrate binding in the absence of the protein, probably by decreasing the repulsion between the polyanionic enzyme and substrate RNAs, and also slow product release and enzyme turnover.

A catalytic RNA and its gene from Salmonella typhimurium.

The gene for the RNA subunit (M1 RNA) of ribonuclease P from Salmonella typhimurium directs the synthesis of an RNA that can cleave transfer RNA precursor molecules. The mature M1 RNA coded for by

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.

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

Tyrosine tRNA precursor molecule polynucleotide sequence.

Evidence suggests that these regions, which can be trimmed in vitro by a nuclease activity in crude cell extracts, are involved in the control of cell tyrosine tRNA levels.

Structure of yeast phenylalanine tRNA at 3 Å resolution

The structure of a tRNA has been determined by isomorphous replacement. Some of the interactions which maintain the tertiary structure are of a novel type. Our model differs significantly from one

Ion dependence of the Bacillus subtilis RNase P reaction.