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

Control of the position of RNase P-mediated transfer RNA precursor processing.

The Journal of biological chemistry - 5 May 1990

Carter B J, Vold B S, Hecht S M

Abstract excerpt

Two Bacillus subtilis tRNA(His) precursors (Green, C. J., and Vold, B. S. (1988) J. Biol. Chem. 263, 652-657) were processed by Escherichia coli RNase P in the presence of varying [Mg2+]. The wild type precursor was processed under all conditions to afford a single tRNA product containing 8 base pairs in the acceptor stem. In contrast, the position of processing of a mutant tRNA(His) precursor (containing a...

Topics

Bacillus subtilis
Base Sequence
Endoribonucleases
Escherichia coli Proteins
Kinetics
Magnesium
Molecular Sequence Data
Mutation
Nucleic Acid Conformation
RNA Processing, Post-Transcriptional
RNA, Transfer, Amino Acid-Specific

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

RNA, Transfer, His

Ribonuclease P

Substrate Specificity

Thermodynamics

Transcription, Genetic

Source

Identifiers

PMID: 2110159

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2110159-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Control of the position of RNase P-mediated transfer RNA precursor processing.PMID 2110159Read ↗

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

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

The pre-tRNA nucleotide base and 2'-hydroxyl at N(-1) contribute to fidelity in tRNA processing by RNase P.Semantic proximity Read ↗

The RNR motif of B. subtilis RNase P protein interacts with both PRNA and pre-tRNA to stabilize an active conformer.Semantic proximity Read ↗

The exocyclic amine at the RNase P cleavage site contributes to substrate binding and catalysis.Semantic proximity Read ↗

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

Role of metal ions in the hydrolysis reaction catalyzed by RNase P RNA from Bacillus subtilis.Semantic proximity Read ↗

The effects of matrices of paired substitutions in mid-acceptor stem on Drosophila tRNA(His) structure and end-processing.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 ↗

Permutation of a pair of tertiary nucleotides in a transfer RNA.Semantic proximity Read ↗

Role of precursor sequences in the ordered maturation of E. coli 23S ribosomal RNA.Semantic proximity Read ↗

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