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Domain IV of elongation factor G from Thermus thermophilus is strictly required for translocation
Author(s) -
Martemyanov Kirill A,
Gudkov Anatoly T
Publication year - 1999
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(99)00635-3
Subject(s) - thermus thermophilus , chromosomal translocation , elongation , domain (mathematical analysis) , elongation factor , thermus , chemistry , biology , genetics , mathematics , gene , bacteria , materials science , escherichia coli , ribosome , rna , ultimate tensile strength , metallurgy , mathematical analysis , thermophile
Two truncated variants of elongation factor G from Thermus thermophilus with deletion of its domain IV have been constructed and the mutated genes were expressed in Escherichia coli . The truncated factors were produced in a soluble form and retained a high thermostability. It was demonstrated that mutated factors possessed (1) a reduced affinity to the ribosomes with an uncleavable GTP analog and (2) a specific ribosome‐dependent GTPase activity. At the same time, in contrast to the wild‐type elongation factor G, they were incapable to promote translocation. The conclusions are drawn that (1) domain IV is not involved in the GTPase activity of elongation factor G, (2) it contributes to the binding of elongation factor G with the ribosome and (3) is strictly required for translocation. These results suggest that domain IV might be directly involved in translocation and GTPase activity of the factor is not directly coupled with translocation.