Open AccessThe Isolation and Characterization of Elongation Factor eEF‐Ts from Krebs‐II Mouse‐Ascites‐Tumor Cells and Its Role in the Elongation Process
Author(s) -
GRASMUK Hans,
NOLAN Robert Dwyer,
DREWS Jürgen
Publication year - 1978
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1978.tb12770.x
Subject(s) - elongation factor , elongation , eukaryotic translation elongation factor 1 alpha 1 , gtp' , ribosome , protein biosynthesis , polysome , biology , microbiology and biotechnology , biochemistry , chemistry , rna , enzyme , materials science , ultimate tensile strength , gene , metallurgy
A factor having activity similar to that described in other systems for the eukaryotic elongation factor eEF‐Ts was isolated from the heavy, aggregate form of eEF‐T H (formally named EF‐1 H ). This protein has a molecular weight of 52000 under native conditions and of 25 500 under denaturing conditions. It has been shown to stimulate eEF‐Tu‐dependent aminoacyl‐tRNA binding to ribosomes and therefore eEF‐Tu/eEF‐G‐dependent polyphenylalanine synthesis by ribosomes and was found to stimulate GDP‐GTP exchange in eEF‐Tu · GDP complexes. In the course of this work, it was also demonstrated that the removal of deacylated tRNA from the ribosome is a GTP‐dependent process. This report, therefore, adds further support to the concept that a third elongation factor, eEF‐Ts, may be common to all systems in the eukaryotic domain.