Title : Elongation factor G stabilizes the hybrid-state conformation of the 70S ribosome.

Pub. Date : 2007 Sep

PMID : 17630323






4 Functional Relationships(s)
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1 Here, we have used a combination of chemical footprinting, peptidyl transferase activity assays, and mRNA toeprinting to monitor the effects of EF-G on the positions of tRNA and mRNA relative to the A, P, and E sites of the ribosome in the presence of GTP, GDP, GDPNP, and fusidic acid. Guanosine Diphosphate G elongation factor mitochondrial 1 Homo sapiens
2 Chemical footprinting experiments show that binding of EF-G in the presence of the non-hydrolyzable GTP analog GDPNP or GDP.fusidic acid induces movement of a deacylated tRNA from the classical P/P state to the hybrid P/E state. Guanosine Diphosphate G elongation factor mitochondrial 1 Homo sapiens
3 A deacylated tRNA bound to the P site and a peptidyl-tRNA in the A site are completely translocated to the E and P sites, respectively, in the presence of EF-G with GTP or GDPNP but not with EF-G.GDP. Guanosine Diphosphate G elongation factor mitochondrial 1 Homo sapiens
4 Our results show that binding of EF-G in the presence of GDPNP or GDP.fusidic acid stabilizes the ribosomal intermediate hybrid state, but that complete translocation is supported only by EF-G.GTP or EF-G.GDPNP. Guanosine Diphosphate G elongation factor mitochondrial 1 Homo sapiens