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A monoclonal antibody specific for carboxy‐terminal region of yeast translation elongation factor‐3 inhibits ribosome‐activated ATPase activity but not intrinsic ATPase activity
Author(s) -
Uritani Masahiro,
Tabata Atsushi,
Nakayama Kazutoshi,
Izuta Miho,
Iizumi Makoto,
Arisawa Mikio
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201231
Subject(s) - elongation factor , ribosome , elongation , translation (biology) , ef tu , atpase , yeast , monoclonal antibody , eukaryotic translation elongation factor 1 alpha 1 , biochemistry , biology , microbiology and biotechnology , chemistry , messenger rna , antibody , rna , enzyme , gene , genetics , materials science , ultimate tensile strength , metallurgy
Elongation factor‐3 (EF‐3) is an essential translation elongation factor specific to yeasts and fungi. When EF‐3 interacts with yeast ribosomes, its ATPase activity, which is indispensable for the function of EF‐3 in translation, is drastically enhanced. In this study, a monoclonal antibody specific for the carboxy‐terminal region inhibited the ribosome‐activated ATPase activity of EF‐3, while it did not inhibit the intrinsic ATPase activity of EF‐3. The results suggest that the carboxy‐terminal region of EF‐3 is involved in the interaction with yeast ribosomes. The monoclonal antibody also inhibited poly(U)‐directed poly(Phe) synthesis, which indicates that the carboxy‐terminal region is important for EF‐3 to express its function in the polypeptide elongation cycle.