Figure 5. Schematic representation of the proposed mechanism for Nmd3 release. The Nmd3-bound 60S subunit in the cytoplasm presents a different conformation compared with the unbound 60S subunit, characterized as the result of a closing motion, as if gripping the ligand Nmd3. The usual multiple binding sites of translational GTPase factors, EF1A, eEF2, eRF3, are in the GAC region, as identified in eukaryotic and prokaryotic systems. In the present 60S complex, this region is partially blocked by the ligand. Thus, the cleft region between CP and GAC, close to the protein Rpl10 region, is a likely binding region for Lsg1. Conformational changes in Lsg1 as well as in the Rpl10-binding cleft, which accompany GTP hydrolysis, allow the 60S subunit to adopt a relaxed conformation and thus facilitate Nmd3 release. Next, the unbound 60S subunit is ready for association with the 40S initiation complex.
Figure 5.

Schematic representation of the proposed mechanism for Nmd3 release. The Nmd3-bound 60S subunit in the cytoplasm presents a different conformation compared with the unbound 60S subunit, characterized as the result of a closing motion, as if gripping the ligand Nmd3. The usual multiple binding sites of translational GTPase factors, EF1A, eEF2, eRF3, are in the GAC region, as identified in eukaryotic and prokaryotic systems. In the present 60S complex, this region is partially blocked by the ligand. Thus, the cleft region between CP and GAC, close to the protein Rpl10 region, is a likely binding region for Lsg1. Conformational changes in Lsg1 as well as in the Rpl10-binding cleft, which accompany GTP hydrolysis, allow the 60S subunit to adopt a relaxed conformation and thus facilitate Nmd3 release. Next, the unbound 60S subunit is ready for association with the 40S initiation complex.

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