Increased functional activity of elongation factor G with G16V mutation in the GTP-binding domain
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Updated: Oct 26, 2026

Xenopus laevis as a Model to Identify Translation Impairment
Published on: September 27, 2015
K A Martemyanov1, A Liljas, A T Gudkov
1Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142292, Russia.
Abstract:
Oligonucleotide-directed mutagenesis was used to obtain elongation factor G from Thermus thermophilus with the G16V mutation in its GTP-binding domain. Functional studies of the mutated protein and elongation factor G from E. coli were carried out. The data revealed that the G16V mutant retains high thermostability, has an increased ribosome-dependent GTPase activity, and its translation activity in cell-free translation system is equal to that of the factor G from E. coli. The mutated protein with an uncleavable GTP analog also has an increased affinity to the ribosomes.
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