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Recognition of tRNAs by aminoacyl‐tRNA synthetases
Author(s) -
Cavarelli Jean,
Moras Dino
Publication year - 1993
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.7.1.8422978
Subject(s) - aminoacyl trna synthetase , transfer rna , computational biology , amino acyl trna synthetases , sequence (biology) , binding site , biology , domain (mathematical analysis) , amino acid , chemistry , biochemistry , rna , mathematics , gene , mathematical analysis
Our present understanding of the molecular mechanisms responsible for the recognition of tRNAs by their cognate aminoacyl‐tRNA synthetases (aaRS) is essentially based on three sources of information: 1 ) the characterization of tRNA identity determinants using in vivo and in vitro approaches, 2 ) the classification of synthetases from primary sequence analysis: aaRS can be partitioned into two classes according to the spatial structure of their ATP binding domain, and 3 ) the structural results of crystallographic investigations and solution studies. The crystal structures of three aaRS and two complexes, one of each class, are known to atomic resolution. tRNA recognition has two structural components. The interaction between the acceptor end and the active site domain is class‐specific and the binding mode of the stem observed in the crystal structures of GlnRS‐tRNA Gln and AspRS‐tRN Asp complexes can be generalized to their respective classes. Identity determinants located in other parts of the tRNA molecule are decoded by different domains of the enzyme. These protein modules exhibit a large structural diversity. The recognition process is then system or subgroup specific.— Gavarelli, J., Moras, D. Recognition of tRNAs by aminoacyl‐tRNA synthetases. FASEB J. 7: 79‐86; 1993.