Human tryptophanyl-tRNA synthetase binds with heme to enhance its aminoacylation activity.

doi:10.1021/bi7012068

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Article

Human tryptophanyl-tRNA synthetase binds with heme to enhance its aminoacylation activity.

Biochemistry - 9 Oct 2007

Wakasugi Keisuke

Abstract excerpt

Mammalian tryptophanyl-tRNA synthetases (TrpRSs) are Zn2+-binding proteins that catalyze the aminoacylation of tRNATrp. The cellular expression level of human TrpRS is highly upregulated by interferon-gamma (IFN-gamma). In this study, a heme biosynthesis inhibitor, succinylacetone (SA), was found to inhibit cellular TrpRS activity in IFN-gamma-activated cells without affecting TrpRS protein expression. In...

Topics

Aminoacylation
Heme
Humans
Models, Molecular
Mutagenesis, Site-Directed
Mutation
Protein Binding
Protein Structure, Secondary
Protein Structure, Tertiary
Tryptophan-tRNA Ligase
Zinc

Source

Open in PubMed

Identifiers

PMID: 17877375
DOI: 10.1021/bi7012068

Provenance

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