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Article

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

Nucleic acids research - 11 Feb 1992

Kirsebom L A, Svärd S G

Abstract excerpt

Cleavage by RNase P of the tRNA(His precursor yields a mature tRNA with an 8 base pair amino acid acceptor stem instead of the usual 7 base pair stem. Here we show, both in vivo and in vitro, that this is mainly dependent on the primary structure and length of the acceptor stem in the precursor. Furthermore, the tRNA(His) precursor used in this study was processed with a change in both kinetic constants, Km and...

Topics

Base Composition
Base Sequence
Endoribonucleases
Escherichia coli
Escherichia coli Proteins
Kinetics
Molecular Sequence Data
Mutation
Nucleic Acid Conformation
RNA Precursors
RNA, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

RNA, Catalytic

RNA, Transfer, His

RNA, Transfer, Tyr

Ribonuclease P

Source

Open in PubMed Open full text

Identifiers

PMID: 1371349
DOI: 10.1093/nar/20.3.425
PMCID: PMC310403

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1371349-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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