Elongation factor G with effector loop from elongation factor Tu is inactive in translocation
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Updated: Oct 2, 2026

Dual DNA Rulers to Study the Mechanism of Ribosome Translocation with Single-Nucleotide Resolution
Published on: July 8, 2019
Alexander Kolesnikov1, Anatoly Gudkov
1Institute of Protein Research, Russian Academy of Sciences, 142290, Moscow Region, Pushchino, Russia.
Abstract:
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.
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