Biopolymers and cell. 2003; 19 (4): 350 - 354

Renaturation of phenylalanyl-tRNA synlhetase by translation elongation factor eEFIA

T. O. Lukash, G. V. Turkovskaya, B. S. Negrutskii, A. V. Elskaya

Translation elongation factor eEFIA provides binding of codon-specific aminoacyl-tRN A to the ribosomal A-site. We report herewith that, in addition to its role in the translation, eEFIA has chaperone-like properties to promote renaturation of denatured phenylalanyl-tRNA synthetase (PheRS). The eEFlA-GDP and eEFIA • GTP complexes demonstrate the same level of activity in stimulating the enzyme renaturation. The eEFIA capacity to pro¬mote renaturation of denatured PheRS might be important for maintenance of the enzyme activity in the protein synthesis compart¬ment in higher eukaryotic cells.