Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The processing of wild type and mutant forms of rat nuclear pre-tRNA(Lys) by the homologous RNase P.

Nucleic acids research - 25 Aug 1994

Paisley T E, Van Tuyle G C

Abstract excerpt

The 5' processing of rat pre-tRNA(Lys) and a series of mutant derivatives by rat cytosolic RNase P was examined. In standard, non-kinetic assays, mutant precursors synthesized in vitro with 5' leader sequences of 10, 17, 24, 25, and 46 nucleotides were processed to approximately equal levels and yielded precisely cleaved 5' processed intermediates with the normal 7-base pair aminoacyl stems. The construct...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Base Sequence
Share to Binding Sites
Share to Kinetics

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Polymerase Chain Reaction

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 8078770
DOI: 10.1093/nar/22.16.3347
PMCID: PMC523728

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The processing of wild type and mutant forms of rat nuclear pre-tRNA(Lys) by the homologous RNase P.PMID 8078770Read ↗

Initiator-elongator discrimination in vertebrate tRNAs for protein synthesis.Semantic proximity Read ↗

Lead-catalyzed cleavage of yeast tRNAPhe mutants.Semantic proximity Read ↗

The kinetics and specificity of cleavage by RNase P is mainly dependent on the structure of the amino acid acceptor stem.Semantic proximity Read ↗

Effects of conserved D/T loop substitutions in the pre-tRNA substrate on tRNase Z catalysis.Semantic proximity Read ↗

Functional replacement of hamster lysyl-tRNA synthetase by the yeast enzyme requires cognate amino acid sequences for proper tRNA recognition.Semantic proximity Read ↗

Recognition of the 5' leader of pre-tRNA substrates by the active site of ribonuclease P.Semantic proximity Read ↗

Genetic methods for study of trans-acting genes involved in processing of precursors to yeast cytoplasmic transfer RNAs.Semantic proximity Read ↗

Plant mitochondrial RNase P and E. coli RNase P have different substrate specificities.Semantic proximity Read ↗

Phosphorothioates in pre-tRNAs can change the specificities of RNAses P or reduce the cleavage efficiencies.Semantic proximity Read ↗

Control of the position of RNase P-mediated transfer RNA precursor processing.Semantic proximity Read ↗

Distribution of both lengths and 5' terminal nucleotides of mammalian pre-tRNA 3' trailers reflects properties of 3' processing endoribonuclease.Semantic proximity Read ↗

The 3' substrate determinants for the catalytic efficiency of the Bacillus subtilis RNase P holoenzyme suggest autolytic processing of the RNase P RNA in vivo.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.