Guanosinetriphosphatase activity dependent on elongation factor Tu and ribosomal protein L7/L12. | Zendy

D. Donner | Zendy; Richard Villems | Zendy; Anders Liljas | Zendy; C. G. Kurland | Zendy

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Guanosinetriphosphatase 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

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.

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