Short Communication THE CLONING AND CHARACTERIZATION OF Tetrahymena pyriformis TRANSLATION ELONGATION FACTOR 1B α AND γ SUBUNITS

The multi-subunit eukaryotic translation elongation factor 1 (eEF1) consists of two functionally distinct parts: G-protein eEF1A and guanine nucleotide exchange factor eEF1B. Here, we report on the cloning of cDNAs of both the α and γ subunits of the eEF1B from the ciliated protozoan Tetrahymena pyriformis. The open reading frame of the eEF1Bγ cDNA encodes a 399-amino acid long polypeptide with a calculated molecular mass of 45.2 kDa. The eEF1Bα cDNA contains an open reading frame encoding a polypeptide of 228 amino acids. The calculated molecular mass of this protein is 25.2 kDa. The overall deduced amino acid sequences of eEF1Bα and eEF1Bγ show a considerable homology with the families of α and γ proteins from other eukaryotic organisms. We demonstrated that eEF1Bγ is an RNA-binding protein which is able to bind to different RNAs.