aminoacyl-tRNA synthetase


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aminoacyl-tRNA synthetase

[ə¦mē·nō¦as·əl ¦tē‚är‚en¦ā ′sin·thə‚tās]
(cell and molecular biology)
An enzyme catalyzing the linkage of a transfer ribonucleic acid (tRNA) molecule to its corresponding amino acid during protein synthesis.
References in periodicals archive ?
th] Annual International Symposium on Aminoacyl-tRNA Synthetases (AARS2015), Barcelona, Spain October 18 -- 22, 2015
Therefore, an RNA-only-based protein synthesis system would require a set of RNA molecules capable of synthesizing aminoacyl-RNAs, which are produced by the protein aminoacyl-tRNA synthetases in extant biology.
Amino acids are covalently attached to their cognate tRNAs through the enzymatic action of aminoacyl-tRNA synthetases.
The focus of the collaboration will be to target specific aminoacyl-tRNA synthetases, a family of 20 enzymes essential to the process of protein translation required for survival of all organisms.
Rodriguez performed many laborious experiments in which she removed portions of the aminoacyl-tRNA synthetase that interact with the anticodon stem of the transfer RNA, far from the part of the enzyme that binds the amino acid.
In all, Rodriguez found that separately removing seven different "gears" from a distant part of the molecule each caused the amino acid to bind more tightly to the aminoacyl-tRNA synthetase.
About Physiocrines Physiocrines are produced from ancient genes, aminoacyl-tRNA synthetases, which are an intercellular gene family involved in protein synthesis.
While the anti-fungal effect of the LeuRS protein inhibition by boron-containing compounds has been established by the clinical results seen for AN2690, other proteins from the same family, known as aminoacyl-tRNA synthetases, are well-validated targets for antibiotic drug development.
Now that we know how AN2690 works, the same approach could be adapted to target other aminoacyl-tRNA synthetases with editing sites, which are also excellent targets for anti-microbial drugs," said Cusack, whose group performed the X-ray crystallography which revealed how AN2690 binds to LeuRS.
The Merck collaboration has focused on discovering novel compounds that inhibit the function of aminoacyl-tRNA synthetases.
9:30 INVESTIGATING TRNA CHANNELING BY AMINOACYL-TRNA SYNTHETASES AND ELONGATION FACTOR TU