Chaperone-like activity of mammalian elongation factor eEF1A: renaturation of aminoacyl-tRNA synthetases

TO Lukash, HV Turkivska, BS Negrutskii… - The international journal …, 2004 - Elsevier
TO Lukash, HV Turkivska, BS Negrutskii, AV El'skaya
The international journal of biochemistry & cell biology, 2004Elsevier
Eukaryotic translational elongation factor eEF1A is known to be responsible for the binding
of codon-specific aminoacyl-tRNAs to the ribosome. In this study, we report that in addition to
this canonical function, eEF1A is able to promote the renaturation of aminoacyl-tRNA
synthetases (ARS) and protect them against denaturation by dilution. The full recovery of the
phenylalanyl-(PheRS) and seryl-tRNA synthetase (SerRS) activities was achieved in the
presence of 4μM eEF1A, while bovine serum albumin at similar concentration had no …
Eukaryotic translational elongation factor eEF1A is known to be responsible for the binding of codon-specific aminoacyl-tRNAs to the ribosome. In this study, we report that in addition to this canonical function, eEF1A is able to promote the renaturation of aminoacyl-tRNA synthetases (ARS) and protect them against denaturation by dilution. The full recovery of the phenylalanyl- (PheRS) and seryl-tRNA synthetase (SerRS) activities was achieved in the presence of 4μM eEF1A, while bovine serum albumin at similar concentration had no renaturation effect. Remarkably, in vitro renaturation occurs at the molar ratio of eEF1A to ARS equivalent to that found in the cytoplasm of higher eukaryotic cells. The eEF1A·GDP and eEF1A·GTP complexes were shown to be similar in their effect on the phenylalanyl-tRNA synthetase renaturation. Thus, we conclude that the chaperone-like activity of eEF1A might be important for maintaining the enzymes activity in the protein synthesis compartments of mammalian cells.
Elsevier
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