Abstract
Ribonuclease P is a ribonucleoprotein that cleaves precursors to transfer RNA (tRNA) molecules to yield the correct 5′ terminal sequences of the mature tRNA's. The RNA moiety M1 RNA 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. When the transcript of the M1 RNA gene is combined with the protein moiety not only is a tRNA precursor cleaved but also the precursor to 4.5 S RNA from Escherichia coli .
Keywords
RNATransfer RNATranscription (linguistics)MoietyEscherichia coliRibonucleasePost-transcriptional modificationRibonucleoproteinChemistryMolecular biologyDegradosomeNon-coding RNARNA editingRNase PBiochemistryMessenger RNABiologyGeneStereochemistry
Affiliated Institutions
Related Publications
Removal of a terminator structure by RNA processing regulates int gene expression
The int gene of phage lambda encodes a protein involved in site-specific recombination. Its expression is regulated differentially during successive phases of the lambda infecti...
Cleavage within an RNase III site can control mRNA stability and protein synthesis<i>in vivo</i>
We report that processing at a cloned bacteriophage T7 RNase III site results in strong stabilization of the mRNA relative to the full-length transcript. In contrast, processing...
Structure of <i>E. coli</i> Glutaminyl-tRNA Synthetase Complexed with tRNA <sup>Gln</sup> and ATP at 2.8 Å Resolution
The crystal structure of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) complexed with its cognate glutaminyl transfer RNA (tRNA Gln ) and adenosine triphosphate (ATP) has ...
Genetic mapping of a mutation that causes ribonucleases III deficiency in Escherichia coli
the mutation that causes ribonuclease III (RNase III) deficiency in strain AB301-105 of Kindler et al. (1973) has been mapped by use of F' merodiploids, Hfr matings, and P1 tran...
Purification of Synthetic Ribonuclease S-Peptide Derivatives by Specific Complex Formation on Columns of Ribonuclease S-Protein Bound to Agarose
Abstract Ribonuclease S-protein was attached covalently to agarose which had been activated by treatment with cyanogen bromide according to the methods described by Porath and h...
Publication Info
- Year
- 1984
- Type
- article
- Volume
- 223
- Issue
- 4633
- Pages
- 285-286
- Citations
- 279
- Access
- Closed
External Links
Social Impact
Altmetric
PlumX Metrics
Social media, news, blog, policy document mentions
Citation Metrics
279
OpenAlex
Cite This
Cecilia Guerrier-Takada,
Sidney Altman
(1984).
Catalytic Activity of an RNA Molecule Prepared by Transcription in Vitro.
Science
, 223
(4633)
, 285-286.
https://doi.org/10.1126/science.6199841
Identifiers
- DOI
- 10.1126/science.6199841