Kinetics and thermodynamics of the RNase P RNA cleavage reaction: analysis of tRNA 3'-end variants.

doi:10.1006/jmbi.1994.0130

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Article

Kinetics and thermodynamics of the RNase P RNA cleavage reaction: analysis of tRNA 3'-end variants.

Journal of molecular biology - 24 Mar 1995

Hardt W D, Schlegl J, Erdmann V A, Hartmann R K

Abstract excerpt

We have studied the interaction of 3'-end variants of a (pre-)tRNAGly with ribonuclease P (RNase P) RNAs from Escherichia coli and Thermus thermophilus. To dissect the thermodynamics of tRNA binding from the overall catalytic reaction, specific binding of mature tRNAGly variants to RNase P RNAs was studied by gel retardation. A newly developed assay, based on the reduction of Pb(2+)-hydrolysis at the CCA end due...

Topics

Base Sequence
Endoribonucleases
Escherichia coli
Escherichia coli Proteins
Genetic Variation
Hydrolysis
Kinetics
Lead
Magnesium
Models, Molecular
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Nucleic Acid Conformation

RNA Processing, Post-Transcriptional

RNA, Bacterial

RNA, Catalytic

RNA, Transfer, Gly

Ribonuclease P

Species Specificity

Source

Open in PubMed

Identifiers

PMID: 7535857
DOI: 10.1006/jmbi.1994.0130

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7535857-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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Kinetics and thermodynamics of the RNase P RNA cleavage reaction: analysis of tRNA 3'-end variants.PMID 7535857Read ↗

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