By Sunghoon Kim
This e-book will specialize in new molecular interactions and novel actions and the linked illnesses which have been lately came upon from the reports of eukaryotic and mammalian aminoacyl-tRNA synthetases. furthermore, the aptitude functions of ARS researches in biotechnology and drugs could be addressed.
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This e-book will concentrate on new molecular interactions and novel actions and the linked illnesses which have been lately chanced on from the reports of eukaryotic and mammalian aminoacyl-tRNA synthetases. moreover, the capability purposes of ARS researches in biotechnology and drugs should be addressed.
Extra resources for Aminoacyl-tRNA Synthetases in Biology and Medicine
9 A crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser). Science 263:1404–1410 Synthetic and Editing Mechanisms of Aminoacyl-tRNA Synthetases 37 137. Borel F, Vincent C, Leberman R, Hartlein M (1994) Seryl-tRNA synthetase from Escherichia coli: implication of its N-terminal domain in aminoacylation activity and specificity. Nucleic Acids Res 22:2963–2969 138. Eriani G, Cavarelli J, Martin F, Dirheimer G, Moras D, Gangloff J (1993) Role of dimerization in yeast aspartyl-tRNA synthetase and importance of the class II invariant proline.
Biochemistry 38:12296–12304 129. Moulinier L, Eiler S, Eriani G, Gangloff J, Thierry JC, Gabriel K, McClain WH, Moras D (2001) The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism. EMBO J 20:5290–5301 130. Onesti S, Desogus G, Brevet A, Chen J, Plateau P, Blanquet S, Brick P (2000) Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding. Biochemistry 39:12853–12861 131. Moor N, Kotik-Kogan O, Tworowski D, Sukhanova M, Safro M (2006) The crystal structure of the ternary complex of phenylalanyl-tRNA synthetase with tRNAPhe and a phenylalanyladenylate analogue reveals a conformational switch of the CCA end.
3 Mechanisms of Pre-transfer Editing The existence of pre-transfer editing was first inferred from early pre-steady state kinetics experiments on IleRS, in which an observed transient accumulation of noncognate Val-tRNAIle was much smaller than expected if the sole pathway were the formation and subsequent hydrolysis of this species . This suggested that hydrolysis of misactivated Val-AMP could account for the observed editing. It was also shown that the half-life of Val-AMP in solution is much longer than the rate of its destruction in these experiments, demonstrating that the proposed reaction is enzyme-catalyzed.
Aminoacyl-tRNA Synthetases in Biology and Medicine by Sunghoon Kim