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

Identity switches between tRNAs aminoacylated by class I glutaminyl- and class II aspartyl-tRNA synthetases.

Biochemistry - 23 Aug 1994

Frugier M, Söll D, Giegé R, Florentz C

Abstract excerpt

High-resolution X-ray structures for the tRNA/aminoacyl-tRNA synthetase complexes between Escherichia coli tRNAGln/GlnRS and yeast tRNAAsp/AspRS have been determined. Positive identity nucleotides that direct aminoacylation specificity have been defined in both cases; E. coli tRNAGln identity is governed by 10 elements scattered in the tRNA structure, while specific aminoacylation of yeast tRNAAsp is dependent on...

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 Kinetics

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

Share to Molecular Sequence Data

Share to Molecular Structure

Share to Mutation

Share to Nucleic Acid Conformation

Share to Saccharomyces cerevisiae

Source

Identifiers

PMID: 8060999
DOI: 10.1021/bi00199a013

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

Identity switches between tRNAs aminoacylated by class I glutaminyl- and class II aspartyl-tRNA synthetases.PMID 8060999Read ↗

Additive, cooperative and anti-cooperative effects between identity nucleotides of a tRNA.Semantic proximity Read ↗

The identity determinants required for the discrimination between tRNAGlu and tRNAAsp by glutamyl-tRNA synthetase from Escherichia coli.Semantic proximity Read ↗

Functional idiosyncrasies of tRNA isoacceptors in cognate and noncognate aminoacylation systems.Semantic proximity Read ↗

Yeast aspartyl-tRNA synthetase residues interacting with tRNA(Asp) identity bases connectively contribute to tRNA(Asp) binding in the ground and transition-state complex and discriminate against non-cognate tRNAs.Semantic proximity Read ↗

Selectivity and specificity in the recognition of tRNA by E coli glutaminyl-tRNA synthetase.Semantic proximity Read ↗

Glutaminyl-tRNA synthetase.Semantic proximity Read ↗

Functional connectivity between tRNA binding domains in glutaminyl-tRNA synthetase.Semantic proximity Read ↗

A non-discriminating aspartyl-tRNA synthetase from Halobacterium salinarum.Semantic proximity Read ↗

The Enzymatic Paradox of Yeast Arginyl-tRNA Synthetase: Exclusive Arginine Transfer Controlled by a Flexible Mechanism of tRNA Recognition.Semantic proximity Read ↗

Glutaminyl-tRNA synthetase: from genetics to molecular recognition.Semantic proximity Read ↗

Single amino acid changes in AspRS reveal alternative routes for expanding its tRNA repertoire in vivo.Semantic proximity Read ↗

Selection of tRNA(Asp) amber suppressor mutants having alanine, arginine, glutamine, and lysine identity.Semantic proximity Read ↗

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