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Aminoacyl-tRNA Synthetases in Biology and Medicine by Sunghoon Kim PDF

By Sunghoon Kim

This publication will concentrate on new molecular interactions and novel actions and the linked illnesses which have been lately stumbled on from the reports of eukaryotic and mammalian aminoacyl-tRNA synthetases. moreover, the aptitude functions of ARS researches in biotechnology and drugs might be addressed.

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Similar substrate-assisted mechanisms based in part on computational studies have been proposed for ProRS, PheRS, and LeuRS [208, 216, 217]. 5 29 Trans Editing Factors Free-standing editing proteins have been discovered that catalyze post-transfer hydrolysis of misacylated tRNA after its dissociation from the aaRS (Fig. 6). In all cases these proteins are homologs of the editing domains of class II aaRS, and constitute a third sieve in the editing process [160]. The finding that product release is rate-limiting for class I editing enzymes, and that class II enzymes are instead rate-limited by an early step in the pathway, helps to rationalize why trans editing generally does not occur in class I systems [46, 97, 159].

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J. Perona and I. Gruic-Sovulj 119. Arnez JG, Harris DC, Mitschler A, Rees B, Francklyn CS, Moras D (1995) Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate. EMBO J 14:4143–4155 120. Banik SD, Nandi N (2010) Aminoacylation reaction in the histidyl-tRNA synthetase: fidelity mechanism of the activation step. J Phys Chem B 114:2301–2311 121. Ng JD, Sauter C, Lorber B, Kirkland N, Arnez J, Giege R (2002) Comparative analysis of space-grown and earth-grown crystals of an aminoacyl-tRNA synthetase: space-grown crystals are more useful for structural determination.

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