[Eukaryotic tryptophanyl-tRNA synthetase acquires affinity to high molecular weight RNA after limited proteolysis].
It is shown that the native tryptophanyl-tRNA synthetase (Mr 2X60 kDa) isolated from bovine pancreas does not interact with high-molecular weight RNAs (E. coli rRNAs). The enzyme acquires the affinity for high-molecular weight RNAs after the cleavage of the 20 kDa fragment from each of the subunits upon digestion by protease. The possible functional significance of the discovered phenomenon is discussed.
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D004926:Escherichia coli / Q000235:genetics; D006868:Hydrolysis; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology; D010447:Peptide Hydrolases; D012313:RNA / Q000378:metabolism*; D012329:RNA, Bacterial / Q000378:metabolism; D014369:Tryptophan-tRNA Ligase / Q000378:metabolism*
D012329:RNA, Bacterial; D012313:RNA; D010447:Peptide Hydrolases; D000604:Amino Acyl-tRNA Synthetases; D014369:Tryptophan-tRNA Ligase
Eukarioticheskaia triptofanil-tRNK-sintetaza priobretaet srodstvo k vysokomolekuliarnym RNK v rezul'tate ogranichennogo proteoliza.