Kushnirov V V, Ter-Avanesyan M D, Surguchov A P, Smirnov V N, Inge-Vechtomov S G
FEBS Lett. 1987 May 11;215(2):257-60. doi: 10.1016/0014-5793(87)80157-6.
Primary structures of yeast sup2 gene and polypeptide product coded by the gene are compared with the current nucleotide and amino acid sequence data base. The amino acid sequence of the sup2 product shows homology to elongation factors from different sources. Especially high homology is found in the regions, corresponding to conservative aminoacyl-tRNA- and GTP-binding domains, described in elongation factors and other proteins. The data obtained are discussed in relation to the functions of sup2 polypeptide product in protein synthesis.