The early history of tRNA recognition by aminoacyl-tRNA synthetases
The early history of tRNA recognition by aminoacyl-tRNA synthetases
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DOI:
10.1007/bf02705187
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发表时间:
2006-10-01
影响因子:
2.9
通讯作者:
Giege, Richard
中科院分区:
文献类型:
--
作者:
Giege, Richard
Discovery of aminoacyl-tRNA synthetases and importance of these enzymes for correct genetic code expression as well as early structural data and related enzymology will be reviewed. Despite structural diversity, all synthetases follow a two-step mechanism for tRNA aminoacylation. Specificity, however, is not absolute since synthetases were shown to catalyze mischarging reactions. These reactions are characterized by low catalytic rates and can lead to incomplete charging levels. Incomplete charging can also occur for cognate tRNA aminoacylation and reflects the equilibrium between the forward acylation and the reverse deacylation (enzymatic and chemical) reactions. Early strategies to characterize the structural features within a given tRNA that account for its preferential aminoacylation by the cognate synthetase will be reviewed. Among them were (i) sequence comparisons of tRNA (RNAs) recognized by a same synthetase,(ii) activity measurements of modified tRNAs (by chemical or enzymatic means) and (iii) reconstitutions of active tRNAs from fragments. As a result, the importance of anticodon and tRNA amino acid accepting arms were highlighted as well as that of the overall tRNA architecture that can be mimicked by tRNA-like structures. Altogether early data gave the robust background to the modern concept of identity.