DnaJC7 binds natively folded structural elements in tau to inhibit amyloid formation

Protein binding by the Hsp70/J-domain protein (JDP) chaperones prevents aggregation of the client protein. Here, the authors show that DnaJC7 binds preferentially to natively folded wild-type tau, via a β-turn element in tau that contains the known amyloid motif, while aggregation-prone tau mutants...

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Autores principales:	Zhiqiang Hou, Pawel M. Wydorski, Valerie A. Perez, Aydé Mendoza-Oliva, Bryan D. Ryder, Hilda Mirbaha, Omar Kashmer, Lukasz A. Joachimiak
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/f2e4491eb9574af5a1fdc65f39a15797
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spelling	oai:doaj.org-article:f2e4491eb9574af5a1fdc65f39a157972021-12-02T14:54:28ZDnaJC7 binds natively folded structural elements in tau to inhibit amyloid formation10.1038/s41467-021-25635-y2041-1723https://doaj.org/article/f2e4491eb9574af5a1fdc65f39a157972021-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25635-yhttps://doaj.org/toc/2041-1723Protein binding by the Hsp70/J-domain protein (JDP) chaperones prevents aggregation of the client protein. Here, the authors show that DnaJC7 binds preferentially to natively folded wild-type tau, via a β-turn element in tau that contains the known amyloid motif, while aggregation-prone tau mutants are recognized with reduced affinity.Zhiqiang HouPawel M. WydorskiValerie A. PerezAydé Mendoza-OlivaBryan D. RyderHilda MirbahaOmar KashmerLukasz A. JoachimiakNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-17 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Zhiqiang Hou Pawel M. Wydorski Valerie A. Perez Aydé Mendoza-Oliva Bryan D. Ryder Hilda Mirbaha Omar Kashmer Lukasz A. Joachimiak DnaJC7 binds natively folded structural elements in tau to inhibit amyloid formation
description	Protein binding by the Hsp70/J-domain protein (JDP) chaperones prevents aggregation of the client protein. Here, the authors show that DnaJC7 binds preferentially to natively folded wild-type tau, via a β-turn element in tau that contains the known amyloid motif, while aggregation-prone tau mutants are recognized with reduced affinity.
format	article
author	Zhiqiang Hou Pawel M. Wydorski Valerie A. Perez Aydé Mendoza-Oliva Bryan D. Ryder Hilda Mirbaha Omar Kashmer Lukasz A. Joachimiak
author_facet	Zhiqiang Hou Pawel M. Wydorski Valerie A. Perez Aydé Mendoza-Oliva Bryan D. Ryder Hilda Mirbaha Omar Kashmer Lukasz A. Joachimiak
author_sort	Zhiqiang Hou
title	DnaJC7 binds natively folded structural elements in tau to inhibit amyloid formation
title_short	DnaJC7 binds natively folded structural elements in tau to inhibit amyloid formation
title_full	DnaJC7 binds natively folded structural elements in tau to inhibit amyloid formation
title_fullStr	DnaJC7 binds natively folded structural elements in tau to inhibit amyloid formation
title_full_unstemmed	DnaJC7 binds natively folded structural elements in tau to inhibit amyloid formation
title_sort	dnajc7 binds natively folded structural elements in tau to inhibit amyloid formation
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/f2e4491eb9574af5a1fdc65f39a15797
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DnaJC7 binds natively folded structural elements in tau to inhibit amyloid formation

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