aminoacyl-tRNA


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a·mi·no·ac·yl-tRNA

(ă-mē'nō-as'il),
Generic term for those compounds in which amino acids are esterfied through their COOH groups to the 3'- (or 2'-) OHs of the terminal adenosine residues of transfer RNAs (for example, alanyl-tRNA, glycyl-tRNA); each compound involves one, or a small number, of tRNAs of specific chemical structure. Used in protein biosynthesis.

aminoacyl-tRNA

the molecule produced when an AMINO ACID is activated into its aminoacyl form and attached to its specific TRANSFER RNA molecule, the whole process being catalysed by a specific aminoacyl-tRNA synthetase enzyme. Also called charged tRNA.
References in periodicals archive ?
The map shows connection of the alanine, aspartate, and glutamate metabolism, arginine and proline metabolism, lysine degradation, phenylalanine metabolism, aminoacyl-tRNA biosynthesis, D- glutamine, and D-glutamate metabolism in human.
The relative yields of the full-length streptavidins obtained in the presence of the BFLAF aminoacyl-tRNA were determined by comparing the band density of the full-length products as compared with those of serially diluted wild type streptavidin.
Ambrogelly et al., "Distinct genetic code expansion strategies for selenocysteine and pyrrolysine are reflected in different aminoacyl-tRNA formation systems," FEBS Letters, vol.
EVALUATING THE INTERACTIONS BETWEEN AMINOACYL-tRNA SYNTHETASES AND ELONGATION FACTOR TU IN PROTEIN SYNTHESIS
This bias exists among the 61 amino acid codons found in mRNA molecules, and the levels of aminoacyl-tRNAs seem to correlate with the frequency of codon usage [3,4].
The enzyme that catalyzes this amino acid-RNA attachment is the aminoacyl-tRNA synthetase.
Autoantibodies against aminoacyl-tRNA synthetase: novel diagnostic marker for type 1 diabetes mellitus.
(3.) Cabanas MJ, Vazquez D, and Modolell J: Dual interference of hygromycin B with ribosomal translocation and with aminoacyl-tRNA recognition.
Directed at new researchers without the benefit of a couple of decades of work in the field, this explains the initial work of Selman Waksman to produce streptomycin, then proceeds to such topics as the biochemistry and genetics of aminoglycoside producers, mechanics of aminoglycoside antibiotic resistance, the development and action of kanamycin and neomycin class antibiotics, NMR structural studies and RNA interaction, structural comparisons between prokaryotic and eukaryotic ribosomal decoding, binding of antibiotics to the aminoacyl-tRNA site of bacterial ribosome, the chemistry and biological relevance of metalloaminoglycosides, adverse effects of aminoglycoside therapy, new efforts at targeting HIV-1 RNA, and novel targets for aminoglycosides.
Our data raise several evolutionary questions, and the first is about the aminoacyl-tRNA synthetases themselves.
Cubist received the milestone payment for developing and transferring technology enabling Bristol-Myers Squibb to target specific aminoacyl-tRNA synthetase enzymes.
To illustrate the power of matching against secondary structure predictions, we present a novel proposed protein alignment, found using this system, for the protein class of aminoacyl-tRNA synthetases.