Open AccessFurther Evidence that Elongation Factor 1 Remains Bound to Ribosomes during Peptide Chain Elongation
Author(s) -
GRASMUK Hans,
NOLAN Robert Dwyer,
DREWS Jürgen
Publication year - 1977
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1977.tb11787.x
Subject(s) - elongation factor , elongation , ribosome , eukaryotic translation elongation factor 1 alpha 1 , protein biosynthesis , biology , peptide , function (biology) , ef tu , microbiology and biotechnology , biochemistry , rna , materials science , ultimate tensile strength , gene , metallurgy
This paper describes three types of experiments which indicate that the binding sites for elongation factor 1 (EF‐1) and elongation factor 2 (EF‐2) on ascites cell ribosomes are not identical and perhaps not even overlapping. The experimental evidence presented includes direct competitive binding of labeled elongation factors to ribosomes as well as the influence of pokeweed antiviral protein and Escherichia coli anti‐L7/L12 proteins on the binding and function of the two factors. It is further shown that EF‐1/β from Artemia salina does not function in displacing EF‐1 from mouse ascites tumor cell ribosomes. These results also support our recently proposed model that EF‐1 remains bound to the ribosome during the peptide chain elongation cycle.