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

tRNA-dependent pre-transfer editing by prokaryotic leucyl-tRNA synthetase.

The Journal of biological chemistry - 29 Jan 2010

Tan Min, Zhu Bin, Zhou Xiao-Long, He Ran, Chen Xin, Eriani Gilbert, Wang En-Duo

Abstract excerpt

To prevent genetic code ambiguity due to misincorporation of amino acids into proteins, aminoacyl-tRNA synthetases have evolved editing activities to eliminate intermediate or final non-cognate products. In this work we studied the different editing pathways of class Ia leucyl-tRNA synthetase (LeuRS). Different mutations and experimental conditions were used to decipher the editing mechanism, including the...

Read the complete abstract on PubMed

Topics

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

Share to Bacteria
Share to Catalysis
Share to Kinetics

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

Share to RNA Editing

Share to RNA, Transfer

Share to RNA, Transfer, Amino Acyl

Share to Sequence Homology, Amino Acid

Share to Tryptophan

Source

Open in PubMed Open full text

Identifiers

PMID: 19940155
DOI: 10.1074/jbc.M109.060616
PMCID: PMC2823433

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

tRNA-dependent pre-transfer editing by prokaryotic leucyl-tRNA synthetase.PMID 19940155Read ↗

Modular pathways for editing non-cognate amino acids by human cytoplasmic leucyl-tRNA synthetase.Semantic proximity Read ↗

The Yin and Yang of tRNA: proper binding of acceptor end determines the catalytic balance of editing and aminoacylation.Semantic proximity Read ↗

A glycine hinge for tRNA-dependent translocation of editing substrates to prevent errors by leucyl-tRNA synthetase.Semantic proximity Read ↗

Identification of essential domains for Escherichia coli tRNA(leu) aminoacylation and amino acid editing using minimalist RNA molecules.Semantic proximity Read ↗

Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability.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 ↗

Mutational unmasking of a tRNA-dependent pathway for preventing genetic code ambiguity.Semantic proximity Read ↗

A Flexible peptide tether controls accessibility of a unique C-terminal RNA-binding domain in leucyl-tRNA synthetases.Semantic proximity Read ↗

Defects in transient tRNA translocation bypass tRNA synthetase quality control mechanisms.Semantic proximity Read ↗

Role of tRNA amino acid-accepting end in aminoacylation and its quality control.Semantic proximity Read ↗

Two tyrosine residues outside the editing active site in Giardia lamblia leucyl-tRNA synthetase are essential for the post-transfer editing.Semantic proximity Read ↗

Quality control by trans-editing factor prevents global mistranslation of non-protein amino acid α-aminobutyrate.Semantic proximity Read ↗

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