Open AccessGuanosinetriphosphatase activity dependent on elongation factor Tu and ribosomal protein L7/L12.
Author(s) -
D. Donner,
Richard Villems,
Anders Liljas,
C. G. Kurland
Publication year - 1978
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.75.7.3192
Subject(s) - elongation factor , ef tu , eukaryotic translation elongation factor 1 alpha 1 , elongation , ribosome , 50s , ribosomal protein , gtpase , ribosomal rna , protein biosynthesis , escherichia coli , biology , gtp' , biochemistry , chemistry , enzyme , rna , materials science , ultimate tensile strength , gene , metallurgy
Incubation of electrophoretically pure samples of the Escherichia coli 50S ribosomal protein L7/L12 together with elongation factor Tu leads to the hydrolysis of GTP. Addition of elongation factor Ts stimulates this reaction. Elongation factor G cannot replace elongation factor Tu for the ribosome-free GTPase reaction dependent on L7/L12. The data suggest that elongation factor Tu and the protein L7/L12 interact directly at the ribosomal A site.