Biopolym. Cell. 2006; 22(1):29-32.
http://dx.doi.org/10.7124/bc.000717
Structure and Function of Biopolymers
Eukaryotic elongation factor 1A disintegrates aggregates of phenylalanyl-tRNA synthetase
1Lukash T. O.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680

Abstract

Translation elongation factor 1A (eEF1A) provides binding and transporting of the appropriate codon-specified aminoacyl-tRNA to the aminoacyl site of the ribosome. Two active tissue-specific isoforms of eEF1A have been identified in mammals. Herewith we report that two isoforms of eEF1A disintegrate the aggregates of phenylalanyl-tRNA synthetase like molecular chaperones which are involved in protein folding and renaturation after stress.
Keywords: translation elongation factor 1A, phenylalanyl-tRNA synthetase, chaperone, aggregation, thermodenaturation
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