Open AccessStability of human recombinant AIMP1/P43 protein in complex with tRNA
Author(s) -
N. V. Vorobyova,
O. Kornelyuk,
Д. М. Ложко
Publication year - 2016
Publication title -
vìsnik. problemi regulâcìï fìzìologìčnih funkcìj/vìsnik kiïvsʹkogo nacìonalʹnogo unìversitetu ìmenì tarasa ševčenka. serìâ: problemi regulâcìï fìzìologìčnih funkcìj
Language(s) - English
Resource type - Journals
eISSN - 2616-6410
pISSN - 1728-2624
DOI - 10.17721/2616_6410.2016.21.49-52
Subject(s) - transfer rna , dissociation constant , intramolecular force , chemistry , recombinant dna , docking (animal) , aminoacyl trna synthetase , titration , dissociation (chemistry) , residue (chemistry) , rna , stereochemistry , biochemistry , organic chemistry , receptor , medicine , nursing , gene
The interaction of AIMP1/р43 recombinant protein, which is a component of aminoacyl-tRNA synthetase complex in higher eukaryotes, in the complex with tRNA was studied. It was shown that temperature stability of AIMP1/p43 is significantly increased in the complex. Local conformational transition of residue Trp271 of AIMP1/p43, which is associated with intramolecular protein stability, is observed at 430C, but in a complex with tRNA it is observed at 490C. Based on the data of spectrofluorimetric titration the value of the dissociation constant and the stoichiometry of the complex of AIMP1/p43 with tRNA were determined. The model of the complex of AIMP1/p43 with tRNA was obtained by the molecular docking method.