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

Recognition by tryptophanyl-tRNA synthetases of discriminator base on tRNATrp from three biological domains.

The Journal of biological chemistry - 19 Apr 2002

Guo Qing, Gong Qingguo, Tong Ka-Lok, Vestergaard Bente, Costa Annie, Desgres Jean, Wong Mansim, Grosjean Henri, Zhu Guang, Wong J Tze-Fei, Xue Hong

Abstract excerpt

To study the recognition by tryptophanyl-tRNA synthetase (TrpRS) of tRNA(Trp) discriminator base, mutations were introduced into the discriminator base of Bacillus subtilis, Archeoglobus fulgidus, and bovine tRNA(Trp), representing the three biological domains. When B. subtilis, A. fulgidus, and human TrpRS were used to acylate these tRNA(Trp), two distinct preference profiles regarding the discriminator base of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cattle
Share to Cloning, Molecular

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

Share to Dose-Response Relationship, Drug

Share to Kinetics

Share to Magnetic Resonance Spectroscopy

Share to Nucleic Acid Conformation

Share to Protein Conformation

Share to Tryptophan

Source

Identifiers

PMID: 11834741
DOI: 10.1074/jbc.M111745200

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

Recognition by tryptophanyl-tRNA synthetases of discriminator base on tRNATrp from three biological domains.PMID 11834741Read ↗

Species-specific differences in the operational RNA code for aminoacylation of tRNA(Trp).Semantic proximity Read ↗

Three G.C base pairs required for the efficient aminoacylation of tRNATrp by tryptophanyl-tRNA synthetase from Bacillus subtilis.Semantic proximity Read ↗

Molecular recognition of tryptophan tRNA by tryptophanyl-tRNA synthetase from Aeropyrum pernix K1.Semantic proximity Read ↗

Tertiary structure base pairs between D- and TpsiC-loops of Escherichia coli tRNA(Leu) play important roles in both aminoacylation and editing.Semantic proximity Read ↗

Threonyl-tRNA synthetase of archaea: importance of the discriminator base in the aminoacylation of threonine tRNA.Semantic proximity Read ↗

Discrimination between transfer-RNAs by tyrosyl-tRNA synthetase.Semantic proximity Read ↗

Modified nucleotides in Bacillus subtilis tRNA(Trp) hyperexpressed in Escherichia coli.Semantic proximity Read ↗

Identity elements of Thermus thermophilus tRNA(Thr).Semantic proximity Read ↗

Two distinct domains of the beta subunit of Aquifex aeolicus leucyl-tRNA synthetase are involved in tRNA binding as revealed by a three-hybrid selection.Semantic proximity Read ↗

A dispensable peptide from Acidithiobacillus ferrooxidans tryptophanyl-tRNA synthetase affects tRNA binding.Semantic proximity Read ↗

Human tryptophanyl-tRNA synthetase is switched to a tRNA-dependent mode for tryptophan activation by mutations at V85 and I311.Semantic proximity Read ↗

Mutations enabling displacement of tryptophan by 4-fluorotryptophan as a canonical amino acid of the genetic code.Semantic proximity Read ↗

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