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An intact conformation at the tip of elongation factor G domain IV is functionally important
Author(s) -
Martemyanov K.A.,
Yarunin A.S.,
Liljas A.,
Gudkov A.T.
Publication year - 1998
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(98)00982-x
Subject(s) - thermus thermophilus , ef tu , gtpase , elongation , elongation factor , chemistry , mutation , ribosome , domain (mathematical analysis) , loop (graph theory) , biochemistry , stereochemistry , biology , biophysics , gene , rna , escherichia coli , mathematical analysis , materials science , mathematics , combinatorics , ultimate tensile strength , metallurgy
Three variants of Thermus thermophilus EF‐G with mutations in the loop at the distal end of its domain IV were obtained. The replacement of His‐573 by Ala and double mutation H573A/D576A did not influence the functional activity of EF‐G. On the other hand, the insertion of six amino acids into the loop between residues Asp‐576 and Ser‐577 reduced the translocational activity of EF‐G markedly, while its GTPase activity was not affected. It is concluded that the native conformation of the loop is important for the factor‐promoted translocation in the ribosome. The functional importance of the entire EF‐G domain IV is discussed.