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Article

Two conserved threonines collaborate in the Escherichia coli leucyl-tRNA synthetase amino acid editing mechanism.

Biochemistry - 29 Nov 2005

Zhai Yuxin, Martinis Susan A

Abstract excerpt

The aminoacyl-tRNA synthetases covalently link transfer RNAs to their cognate amino acids. Some of the tRNA synthetases have employed an editing mechanism to ensure fidelity in this first step of protein synthesis. The amino acid editing active site for Escherichia coli leucyl-tRNA synthetase resides within the CP1 domain that folds discretely from the main body of the enzyme. A portion of the editing active site...

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Identifiers

PMID: 16300391
DOI: 10.1021/bi0514461

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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.

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Two conserved threonines collaborate in the Escherichia coli leucyl-tRNA synthetase amino acid editing mechanism.PMID 16300391Read ↗

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 ↗

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

A glycine hinge for tRNA-dependent translocation of editing substrates to prevent errors by 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 ↗

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

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

Transfer RNA-mediated editing in threonyl-tRNA synthetase. The class II solution to the double discrimination problem.Semantic proximity Read ↗

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Translational fidelity maintenance preventing Ser mis-incorporation at Thr codon in protein from eukaryote.Semantic proximity Read ↗

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

A viable amino acid editing activity in the leucyl-tRNA synthetase CP1-splicing domain is not required in the yeast mitochondria.Semantic proximity Read ↗

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