Elongation factor G stabilizes the hybrid-state conformation of the 70S ribosome - PubMed (original) (raw)

Chemical footprinting of a ribosome·tRNAPhe·EF-G·(GTP/GDP)·fusidic acid complex. Lanes A, C, and G, sequencing lanes; lane K, unmodified rRNA; lane 1, 70S ribosomes and mRNA32; lane 2, 70S ribosomes, mRNA32, and _N_-Ac-Phe-tRNAPhe, and puromycin; lane 3, 70S ribosomes, mRNA32, _N_-Ac-Phe-tRNAPhe, puromycin, and EF-G·GTP; lane 4, 70S ribosomes, mRNA32, _N_-Ac-Phe-tRNAPhe, puromycin, EF-G·GTP, and fusidic acid; lane 5, 70S ribosomes, mRNA32, _N_-Ac-Phe-tRNAPhe, puromycin, and EF-G·GDPNP; lane 6, 70S ribosomes, mRNA32, _N_-Ac-Phe-tRNAPhe, puromycin, and EF-G·GDP; lane 7, 70S ribosomes, mRNA32, _N_-Ac-Phe-tRNAPhe, puromycin, EF-G·GDP, and fusidic acid. (A) 16S rRNA P site; (B) 23S rRNA P site; (C) 23S rRNA E site; (D) 16S rRNA inter-subunit bridge B7a; (E) 23S rRNA sarcin–ricin loop (SRL, EF-G binding site); (F) 23S rRNA

G

TPase-

a

ssociated

c

enter (GAC, EF-G binding site); (G) schematic indicating movement of tRNAPhe in the presence of EF-G·(GTP or GDP)·fusidic acid.