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Information × Registration Number 0209U010819, 0105U003263 , R & D reports Title Study on molecular mechanisms of aminoacyl-tRNA synthetase edyting activity. popup.stage_title Head Tukalo Mykhaylo, Доктор біологічних наук Registration Date 29-12-2009 Organization Institute of molecular biology & genetics popup.description2 Crystall structure of T.thermophilus LeuRSTT:tRNALeu complex has been studied. Obtained data supplemented with results of previous studied SerRS : тРНКSer and TyrRS : tRNATyr complexes allowed to understand mechanisms of recognition of tRNAs with a long variable stem by their cognate aminoacyl-tRNA synthetases. The role of the structural differences between tRNASer, tRNATyr and tRNALeu in recognition processes have been shown. Correspondence of crystall structures of tRNALeu and tRNATyr with theire tertiary structures in solutions have been found. Structures of obtained complexes of LeuRSTT:tRNALeu allowed to create a model of participation of tRNALeu in aminoacylation and post-transfer editing. The model of the interaction of 3'-end of tRNALeu with aminoacylation active site of LeuRSTT have been proposed. Based on studies of mutant forms of enzyme as well as derivatives of tRNA, tRNA-dependent mechanisms of pre- and post-transfer editing have been found in which an important role of 2'- and 3'-OH groups of tRNA have suggested. Crystals of E. faecalis ProRS and their complexes with low-molecular substrates and two isoaccepting tRNAPro was obtained. Structures of E. faecalis and ProRSs was studied by the X-ray analysis method. Model of complex E. faecalis ProRS:tRNAPro and model of editing active site of E. faecalis ProRS have been propoused and have been tested by site-directed mutagenesis method. Product Description popup.authors Гудзера Ольга Йосипівна, Коваленко Оксана Петрівна Крикливий Іван Андрійович Яремчук Ганна Дмитрівна popup.nrat_date 2020-04-02 Close