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The Role of Guanosine Triphosphate in Translocation Reaction Catalyzed by Elongation Factor G

From the ¹ From the Institute of Medical Science, University of Tokyo, Takanawa, Minatoku, Tokyo

The role of GTP in the translocation reaction catalyzed by elongation factor G (EF-G) has been investigated. The addition of EF-G and GTP to a poly(U)-ribosome complex having deacylated tRNA in the P site and N-acetyldiphenyl-alanyl-tRNA in the A site (Complex II) results in the shift of N-acetyldiphenylalanyl-tRNA from the A to the P site of ribosomes with a concomitant release of tRNA from the P site.

It was found that 5'-guanylylmethylenediphosphonate (Gpp(CH₂)p), a nonhydrolyzable analog of GTP, could substitute for GTP in this reaction provided that a stoichiometric amount of EF-G is employed. When Complex II was incubated with a stoichiometric amount of EF-G and Gpp(CH₂)p, the deacylated tRNA was released from the P site and the N-acetyldiphenylalanyl-tRNA in the A site was shifted to the P site to become puromycin-reactive.

It is concluded that the role of GTP in this reaction is to facilitate the binding of EF-G to Complex II. The translocation reaction is promoted probably by conformational change of Complex II induced through interaction with EF-G and GTP. The hydrolysis of GTP appears to be required for the removal of EF-G after completion of the translocation reaction.

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