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CTP can replace GTP in reactions catalyzed by eukaryotic peptide elongation factor 1
Author(s) -
Tuháčková Z.,
Havránek M.,
Hradec J.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80992-8
Subject(s) - gtp' , elongation factor , ef tu , gtpase , autophosphorylation , ribosome , biochemistry , chemistry , eukaryotic translation elongation factor 1 alpha 1 , peptide , elongation , microbiology and biotechnology , biology , phosphorylation , rna , protein kinase a , enzyme , ultimate tensile strength , metallurgy , gene , materials science
In several reactions catalyzed by highly purified peptide elongation factor 1 from rabbit reticulocytes, GTP may be fully replaced by CTP but not by ATP or UTP. This holds true for the factor‐dependent binding of aminoacyl‐tRNA to ribosomes, GTPase activity, GTP‐dependent autophosphorylation of the factor protein and binding of cholesteryl 14‐methylhexadecanoate by the factor.