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 covalen...

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Autores principales:	Fuxing Zeng, Hong Jin
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0779fdb0ae3b4c1fa8fd891756629555
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spelling	oai:doaj.org-article:0779fdb0ae3b4c1fa8fd8917566295552021-12-02T15:07:50ZConformation of methylated GGQ in the Peptidyl Transferase Center during Translation Termination10.1038/s41598-018-20107-82045-2322https://doaj.org/article/0779fdb0ae3b4c1fa8fd8917566295552018-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-20107-8https://doaj.org/toc/2045-2322Abstract 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 among otherwise unrelated proteins that catalyze peptide release. The requirement for this tripeptide in the highly conserved peptidyl transferase center suggests that the conformation reported here is likely shared during termination of protein synthesis in all domains of life.Fuxing ZengHong JinNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-7 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Fuxing Zeng Hong Jin Conformation of methylated GGQ in the Peptidyl Transferase Center during Translation Termination
description	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 among otherwise unrelated proteins that catalyze peptide release. The requirement for this tripeptide in the highly conserved peptidyl transferase center suggests that the conformation reported here is likely shared during termination of protein synthesis in all domains of life.
format	article
author	Fuxing Zeng Hong Jin
author_facet	Fuxing Zeng Hong Jin
author_sort	Fuxing Zeng
title	Conformation of methylated GGQ in the Peptidyl Transferase Center during Translation Termination
title_short	Conformation of methylated GGQ in the Peptidyl Transferase Center during Translation Termination
title_full	Conformation of methylated GGQ in the Peptidyl Transferase Center during Translation Termination
title_fullStr	Conformation of methylated GGQ in the Peptidyl Transferase Center during Translation Termination
title_full_unstemmed	Conformation of methylated GGQ in the Peptidyl Transferase Center during Translation Termination
title_sort	conformation of methylated ggq in the peptidyl transferase center during translation termination
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/0779fdb0ae3b4c1fa8fd891756629555
work_keys_str_mv	AT fuxingzeng conformationofmethylatedggqinthepeptidyltransferasecenterduringtranslationtermination AT hongjin conformationofmethylatedggqinthepeptidyltransferasecenterduringtranslationtermination
_version_	1718388363599282176

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

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