Proline/arginine dipeptide repeat polymers derail protein folding in amyotrophic lateral sclerosis

The most frequent cause of familial Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal Dementia (FTD) are hexanucleotide repeat expansions in the non-coding region of the C9ORF72 gene that are translated into five dipeptide repeat (DPR) proteins. Here, the authors show that proline/arginine (PR)...

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Autores principales:	Maria Babu, Filippo Favretto, Alain Ibáñez de Opakua, Marija Rankovic, Stefan Becker, Markus Zweckstetter
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/5671eab95f98401cbdffa726c9e3c6c6
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spelling	oai:doaj.org-article:5671eab95f98401cbdffa726c9e3c6c62021-12-02T17:34:47ZProline/arginine dipeptide repeat polymers derail protein folding in amyotrophic lateral sclerosis10.1038/s41467-021-23691-y2041-1723https://doaj.org/article/5671eab95f98401cbdffa726c9e3c6c62021-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-23691-yhttps://doaj.org/toc/2041-1723The most frequent cause of familial Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal Dementia (FTD) are hexanucleotide repeat expansions in the non-coding region of the C9ORF72 gene that are translated into five dipeptide repeat (DPR) proteins. Here, the authors show that proline/arginine (PR) DPRs inhibit the prolyl isomerase PPIA and reveal the molecular mechanism of the impaired protein folding activity of PPIA by performing NMR measurements and determining a PR DPR bound PPIA crystal structure.Maria BabuFilippo FavrettoAlain Ibáñez de OpakuaMarija RankovicStefan BeckerMarkus ZweckstetterNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-7 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Maria Babu Filippo Favretto Alain Ibáñez de Opakua Marija Rankovic Stefan Becker Markus Zweckstetter Proline/arginine dipeptide repeat polymers derail protein folding in amyotrophic lateral sclerosis
description	The most frequent cause of familial Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal Dementia (FTD) are hexanucleotide repeat expansions in the non-coding region of the C9ORF72 gene that are translated into five dipeptide repeat (DPR) proteins. Here, the authors show that proline/arginine (PR) DPRs inhibit the prolyl isomerase PPIA and reveal the molecular mechanism of the impaired protein folding activity of PPIA by performing NMR measurements and determining a PR DPR bound PPIA crystal structure.
format	article
author	Maria Babu Filippo Favretto Alain Ibáñez de Opakua Marija Rankovic Stefan Becker Markus Zweckstetter
author_facet	Maria Babu Filippo Favretto Alain Ibáñez de Opakua Marija Rankovic Stefan Becker Markus Zweckstetter
author_sort	Maria Babu
title	Proline/arginine dipeptide repeat polymers derail protein folding in amyotrophic lateral sclerosis
title_short	Proline/arginine dipeptide repeat polymers derail protein folding in amyotrophic lateral sclerosis
title_full	Proline/arginine dipeptide repeat polymers derail protein folding in amyotrophic lateral sclerosis
title_fullStr	Proline/arginine dipeptide repeat polymers derail protein folding in amyotrophic lateral sclerosis
title_full_unstemmed	Proline/arginine dipeptide repeat polymers derail protein folding in amyotrophic lateral sclerosis
title_sort	proline/arginine dipeptide repeat polymers derail protein folding in amyotrophic lateral sclerosis
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/5671eab95f98401cbdffa726c9e3c6c6
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Proline/arginine dipeptide repeat polymers derail protein folding in amyotrophic lateral sclerosis

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