Chaperone activation and client binding of a 2-cysteine peroxiredoxin

Many 2-Cystein Peroxiredoxins (Prx) can either function as peroxidases or chaperones when exposed to stress. Here the authors present the structures of Leishmania infantum mitochondrial Prx alone and with a bound model client protein, use crosslinking to reveal interaction regions that stabilize the...

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Autores principales:	Filipa Teixeira, Eric Tse, Helena Castro, Karl A. T. Makepeace, Ben A. Meinen, Christoph H. Borchers, Leslie B. Poole, James C. Bardwell, Ana M. Tomás, Daniel R. Southworth, Ursula Jakob
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/df1a8fb0297f4c10ab0f61d7773553d4
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spelling	oai:doaj.org-article:df1a8fb0297f4c10ab0f61d7773553d42021-12-02T14:39:18ZChaperone activation and client binding of a 2-cysteine peroxiredoxin10.1038/s41467-019-08565-82041-1723https://doaj.org/article/df1a8fb0297f4c10ab0f61d7773553d42019-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-08565-8https://doaj.org/toc/2041-1723Many 2-Cystein Peroxiredoxins (Prx) can either function as peroxidases or chaperones when exposed to stress. Here the authors present the structures of Leishmania infantum mitochondrial Prx alone and with a bound model client protein, use crosslinking to reveal interaction regions that stabilize the bound client, and provide insights into the mechanism by which Prx’s adopt chaperone activity.Filipa TeixeiraEric TseHelena CastroKarl A. T. MakepeaceBen A. MeinenChristoph H. BorchersLeslie B. PooleJames C. BardwellAna M. TomásDaniel R. SouthworthUrsula JakobNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Filipa Teixeira Eric Tse Helena Castro Karl A. T. Makepeace Ben A. Meinen Christoph H. Borchers Leslie B. Poole James C. Bardwell Ana M. Tomás Daniel R. Southworth Ursula Jakob Chaperone activation and client binding of a 2-cysteine peroxiredoxin
description	Many 2-Cystein Peroxiredoxins (Prx) can either function as peroxidases or chaperones when exposed to stress. Here the authors present the structures of Leishmania infantum mitochondrial Prx alone and with a bound model client protein, use crosslinking to reveal interaction regions that stabilize the bound client, and provide insights into the mechanism by which Prx’s adopt chaperone activity.
format	article
author	Filipa Teixeira Eric Tse Helena Castro Karl A. T. Makepeace Ben A. Meinen Christoph H. Borchers Leslie B. Poole James C. Bardwell Ana M. Tomás Daniel R. Southworth Ursula Jakob
author_facet	Filipa Teixeira Eric Tse Helena Castro Karl A. T. Makepeace Ben A. Meinen Christoph H. Borchers Leslie B. Poole James C. Bardwell Ana M. Tomás Daniel R. Southworth Ursula Jakob
author_sort	Filipa Teixeira
title	Chaperone activation and client binding of a 2-cysteine peroxiredoxin
title_short	Chaperone activation and client binding of a 2-cysteine peroxiredoxin
title_full	Chaperone activation and client binding of a 2-cysteine peroxiredoxin
title_fullStr	Chaperone activation and client binding of a 2-cysteine peroxiredoxin
title_full_unstemmed	Chaperone activation and client binding of a 2-cysteine peroxiredoxin
title_sort	chaperone activation and client binding of a 2-cysteine peroxiredoxin
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/df1a8fb0297f4c10ab0f61d7773553d4
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Chaperone activation and client binding of a 2-cysteine peroxiredoxin

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