Biopolym. Cell. 2003; 19(4):350-354.
Structure and Function of Biopolymers
Renaturation of phenylalanyl-tRNA synlhetase by translation elongation factor eEF1A
1Lukash T. O., 1Turkovskaya G. V., 1Negrutskii B. S., 1El'skaya A. V.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680


Translation elongation factor eEF1A provides binding of codon-specific aminoacyl-tRNA to the ribosomal A-site. We report herewith that, in addition to its role in the translation, eEF1A has chaperone-like properties to promote renaturation of denatured phenylalanyl-tRNA synthetase (PheRS). The eEF1A·GDP and eEF1A · GTP complexes demonstrate the same level of activity in stimulating the enzyme renaturation. The eEF1A capacity to promote renaturation of denatured PheRS might be important for maintenance of the enzyme activity in the protein synthesis compartment in higher eukaryotic cells.


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