Nascent chains can form co-translational folding intermediates that promote post-translational folding outcomes in a disease-causing protein

Alpha-1-antitrypsin (AAT) deficiency results from misfolding-prone AAT variants. Here the authors show that AAT forms co-translational folding intermediates on the ribosome that persist upon release and determine its folding fate. They show too that the ribosome can also modulate misfolding-prone AA...

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Autores principales:	Elena Plessa, Lien P. Chu, Sammy H. S. Chan, Oliver L. Thomas, Anaïs M. E. Cassaignau, Christopher A. Waudby, John Christodoulou, Lisa D. Cabrita
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/30b1313e15054f30a9de5b5032f07b04
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spelling	oai:doaj.org-article:30b1313e15054f30a9de5b5032f07b042021-11-14T12:34:38ZNascent chains can form co-translational folding intermediates that promote post-translational folding outcomes in a disease-causing protein10.1038/s41467-021-26531-12041-1723https://doaj.org/article/30b1313e15054f30a9de5b5032f07b042021-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-26531-1https://doaj.org/toc/2041-1723Alpha-1-antitrypsin (AAT) deficiency results from misfolding-prone AAT variants. Here the authors show that AAT forms co-translational folding intermediates on the ribosome that persist upon release and determine its folding fate. They show too that the ribosome can also modulate misfolding-prone AAT intermediates during their synthesis.Elena PlessaLien P. ChuSammy H. S. ChanOliver L. ThomasAnaïs M. E. CassaignauChristopher A. WaudbyJohn ChristodoulouLisa D. CabritaNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Elena Plessa Lien P. Chu Sammy H. S. Chan Oliver L. Thomas Anaïs M. E. Cassaignau Christopher A. Waudby John Christodoulou Lisa D. Cabrita Nascent chains can form co-translational folding intermediates that promote post-translational folding outcomes in a disease-causing protein
description	Alpha-1-antitrypsin (AAT) deficiency results from misfolding-prone AAT variants. Here the authors show that AAT forms co-translational folding intermediates on the ribosome that persist upon release and determine its folding fate. They show too that the ribosome can also modulate misfolding-prone AAT intermediates during their synthesis.
format	article
author	Elena Plessa Lien P. Chu Sammy H. S. Chan Oliver L. Thomas Anaïs M. E. Cassaignau Christopher A. Waudby John Christodoulou Lisa D. Cabrita
author_facet	Elena Plessa Lien P. Chu Sammy H. S. Chan Oliver L. Thomas Anaïs M. E. Cassaignau Christopher A. Waudby John Christodoulou Lisa D. Cabrita
author_sort	Elena Plessa
title	Nascent chains can form co-translational folding intermediates that promote post-translational folding outcomes in a disease-causing protein
title_short	Nascent chains can form co-translational folding intermediates that promote post-translational folding outcomes in a disease-causing protein
title_full	Nascent chains can form co-translational folding intermediates that promote post-translational folding outcomes in a disease-causing protein
title_fullStr	Nascent chains can form co-translational folding intermediates that promote post-translational folding outcomes in a disease-causing protein
title_full_unstemmed	Nascent chains can form co-translational folding intermediates that promote post-translational folding outcomes in a disease-causing protein
title_sort	nascent chains can form co-translational folding intermediates that promote post-translational folding outcomes in a disease-causing protein
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/30b1313e15054f30a9de5b5032f07b04
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Nascent chains can form co-translational folding intermediates that promote post-translational folding outcomes in a disease-causing protein

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