The stoichiometry of ribosomal translocation.
作者： Juan Modolell , Bartolomé Cabrer , David Vázquez
DOI: 10.1016/S0021-9258(19)43140-2
关键词:
摘要: Abstract Fusidic acid does not inhibit the translocation of N-acetylphenylalanyl-tRNA (N-acetyl-Phe-tRNA), bound nonenzymically to ribosomal A-site, when amount ribosomes in reaction mixture is sufficient trap all available elongation factor G (EF-G) form GDP ·EF-G ·fusidic ·ribosome complexes. Moreover, since only those that are devoid N-acetyl-Phe-tRNA this complex, their strong, uncoupled EF G-dependent GTP hydrolysis inhibited by presence and associated with fraction charged can be detected. After correction for limited due formation GDP·EF-G·fusidic acid·ribosome complex on uncharged ribosomes, it found 1 molecule hydrolyzed per translocated.
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