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Elongation factor G with effector loop from elongation factor Tu is inactive in translocation
Author(s) -
Kolesnikov Alexander,
Gudkov Anatoly
Publication year - 2002
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/s0014-5793(02)02300-1
Subject(s) - elongation factor , elongation , effector , gtpase , ef tu , ribosome , chromosomal translocation , microbiology and biotechnology , loop (graph theory) , protein biosynthesis , biology , chemistry , biophysics , biochemistry , rna , gene , materials science , mathematics , combinatorics , ultimate tensile strength , metallurgy
Elongation factors Tu and G (EF‐Tu and EF‐G) alternately interact with the ribosome during the elongation phase of protein biosynthesis. The function of both factors depends on GTP binding, and the factors are ascribed to a superfamily of G‐proteins . All G‐proteins contain the effector loop, a structural element that is important for the protein's interaction with its target molecule. In this study the effector loop of EF‐G was replaced by the loop taken from EF‐Tu. The EF‐G with EF‐Tu loop has markedly decreased GTPase activity and did not catalyze translocation. We conclude that these loops are not functionally interchangeable since the factors interact with different states of the ribosome.