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

Sequence changes in both flanking sequences of a pre-tRNA influence the cleavage specificity of RNase P.

Journal of molecular biology - 20 Feb 1991

Krupp G, Kahle D, Vogt T, Char S

Abstract excerpt

The cleavage specificities of the RNase P holoenzymes from Escherichia coli and the yeast Schizosaccharomyces pombe and of the catalytic M1 RNA from E. coli were analyzed in 5'-processing experiments using a yeast serine pre-tRNA with mutations in both flanking sequences. The template DNAs were obtained by enzymatic reactions in vitro and transcribed with phage SP6 or T7 RNA polymerase. The various mutations did...

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 Escherichia coli
Share to Escherichia coli Proteins

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

Share to Molecular Sequence Data

Share to Mutation

Share to Nucleic Acid Conformation

Share to Substrate Specificity

Share to Transcription, Genetic

Source

Identifiers

PMID: 1706437
DOI: 10.1016/0022-2836(91)90522-8

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

Sequence changes in both flanking sequences of a pre-tRNA influence the cleavage specificity of RNase P.PMID 1706437Read ↗

Identification of a region within M1 RNA of Escherichia coli RNase P important for the location of the cleavage site on a wild-type tRNA precursor.Semantic proximity Read ↗

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

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

Characterization of conserved sequence elements in eukaryotic RNase P RNA reveals roles in holoenzyme assembly and tRNA processing.Semantic proximity Read ↗

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

Enzymatic formation of modified nucleosides in tRNA: dependence on tRNA architecture.Semantic proximity Read ↗

In vitro genetic analysis of the structural features of the pre-tRNA required for determination of the 3' splice site in the intron excision reaction.Semantic proximity Read ↗

The peculiar architectural framework of tRNASec is fully recognized by yeast AspRS.Semantic proximity Read ↗

Analysis of the functional modules of the tRNA 3' endonuclease (tRNase Z).Semantic proximity Read ↗

Cleavage of pre-tRNAs by the splicing endonuclease requires a composite active site.Semantic proximity Read ↗

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