[Aminoacyl-tRNA synthetases (codases) and their noncanonical functions].
The aim of this review is to summarize the data obtained in the author's laboratory during the last decade. The main objects of these investigations were mammalian aminoacyl-tRNA synthetases, mainly bovine tryptophanyl-tRNA synthetase (EC 6.1.1.2). The data are discussed and compared with those described in literature. In the course of these studies it turned out that some properties of mammalian aminoacyl-tRNA synthetases for instance, nuclear location of some of the synthetases, presence of extra-domain in bovine tryptophanyl-tRNA synthetase capable of catalyzing hydrolysis of ATP and GTP in the absence of Zn2+ ions and normal aminoacylation capacity, ability to bind to one of the glycolytic enzymes, glyceraldehyde-3-phosphate dehydrogenase, formation of aminoacylated and pyrophosphorylated forms of tryptophanyl-tRNA synthetase etc., seem to be unrelated to the main function of the synthetases, catalysis of aminoacyl-tRNA formation, and, therefore, might be classified as noncanonical ones. Comparison of prokaryotic and eukaryotic aminoacyl-tRNA synthetases indicates the multipotential nature of the latter.
Kiselev
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D000255:Adenosine Triphosphate / Q000378:metabolism; D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism / Q000502:physiology*; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D002417:Cattle; D006160:Guanosine Triphosphate / Q000378:metabolism; D006868:Hydrolysis; D007150:Immunohistochemistry; D014369:Tryptophan-tRNA Ligase / Q000378:metabolism / Q000502:physiology
D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D000604:Amino Acyl-tRNA Synthetases; D014369:Tryptophan-tRNA Ligase
Aminoatsil-tRNK sintetazy (kodazy) i ik nekanonicheskie funtstii.