Premium
Arginines 29 and 59 of elongation factor G are important for GTP hydrolysis or translocation on the ribosome
Author(s) -
Mohr Dagmar,
Wintermeyer Wolfgang,
Rodnina Marina V.
Publication year - 2000
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/19.13.3458
Subject(s) - gtpase , gtp' , ribosome , elongation factor , biochemistry , ef tu , arginine , chemistry , microbiology and biotechnology , chromosomal translocation , biology , biophysics , amino acid , enzyme , rna , gene
GTP hydrolysis by elongation factor G (EF‐G) is essential for the translocation step in protein elongation. The low intrinsic GTPase activity of EF‐G is strongly stimulated by the ribosome. Here we show that a conserved arginine, R29, of Escherichia coli EF‐G is crucial for GTP hydrolysis on the ribosome, but not for GTP binding or ribosome interaction, suggesting that it may be directly involved in catalysis. Another conserved arginine, R59, which is homologous to the catalytic arginine of G α proteins, is not essential for GTP hydrolysis, but influences ribosome binding and translocation. These results indicate that EF‐G is similar to other GTPases in that an arginine residue is required for GTP hydrolysis, although the structural changes leading to GTPase activation are different.