Conformation of methylated GGQ in the Peptidyl Transferase Center during Translation Termination.

ABSTRACT: The universally conserved Gly-Gly-Gln (GGQ) tripeptide in release factors or release factor-like surveillance proteins is required to catalyze the release of nascent peptide in the ribosome. The glutamine of the GGQ is methylated post-translationally at the N⁵ position in vivo; this covalent modification is essential for optimal cell growth and efficient translation termination. However, the precise conformation of the methylated-GGQ tripeptide in the ribosome remains unknown. Using cryoEM and X-ray crystallography, we report the conformation of methylated-GGQ in the peptidyl transferase center of the ribosome during canonical translational termination and co-translation quality control. It has been suggested that the GGQ motif arose independently through convergent evolution am

SUBMITTER: Zeng F 

PROVIDER: S-EPMC5799190 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature