The accuracy of aminoacylation--ensuring the fidelity of the genetic code.
The fidelity of protein biosynthesis rests not only on the proper interaction of the messenger RNA codon with the anticodon of the tRNA, but also on the correct attachment of amino acids to their corresponding (cognate) transfer RNA (tRNA) species. This process is catalyzed by the aminoacyl-tRNA synthetases which discriminate with remarkable selectivity amongst many structurally similar tRNAs. The basis for this highly specific recognition of tRNA by these enzymes (also referred to as 'tRNA identity') is currently being elucidated by genetic, biochemical and biophysical techniques. At least two factors are important in determining the accuracy of aminoacylation: a) 'identity elements' in tRNA denote nucleotides in certain positions crucial for protein interactions determining specificity, and b) the occurrence in vivo of competition between synthetases for a particular tRNA which may have ambiguous identity.
Söll
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Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511.
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism* / Q000648:ultrastructure; D001483:Base Sequence; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D016153:Genes, Suppressor; D005815:Genetic Code; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation; D012351:RNA, Transfer, Gln / Q000235:genetics / Q000378:metabolism*; D013329:Structure-Activity Relationship; D046249:Transfer RNA Aminoacylation
D012351:RNA, Transfer, Gln; D000604:Amino Acyl-tRNA Synthetases