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...

Full description

Bibliographic Details
Main Authors:	Zhiqiang Hou, Pawel M. Wydorski, Valerie A. Perez, Aydé Mendoza-Oliva, Bryan D. Ryder, Hilda Mirbaha, Omar Kashmer, Lukasz A. Joachimiak
Format:	Article
Language:	English
Published:	Nature Publishing Group 2021-09-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-021-25635-y

id	doaj-f2e4491eb9574af5a1fdc65f39a15797
record_format	Article
spelling	doaj-f2e4491eb9574af5a1fdc65f39a157972021-09-12T11:46:46ZengNature Publishing GroupNature Communications2041-17232021-09-0112111710.1038/s41467-021-25635-yDnaJC7 binds natively folded structural elements in tau to inhibit amyloid formationZhiqiang Hou0Pawel M. Wydorski1Valerie A. Perez2Aydé Mendoza-Oliva3Bryan D. Ryder4Hilda Mirbaha5Omar Kashmer6Lukasz A. Joachimiak7Center for Alzheimer’s and Neurodegenerative Diseases, University of Texas Southwestern Medical CenterCenter for Alzheimer’s and Neurodegenerative Diseases, University of Texas Southwestern Medical CenterCenter for Alzheimer’s and Neurodegenerative Diseases, University of Texas Southwestern Medical CenterCenter for Alzheimer’s and Neurodegenerative Diseases, University of Texas Southwestern Medical CenterCenter for Alzheimer’s and Neurodegenerative Diseases, University of Texas Southwestern Medical CenterCenter for Alzheimer’s and Neurodegenerative Diseases, University of Texas Southwestern Medical CenterCenter for Alzheimer’s and Neurodegenerative Diseases, University of Texas Southwestern Medical CenterCenter for Alzheimer’s and Neurodegenerative Diseases, University of Texas Southwestern Medical CenterProtein 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.https://doi.org/10.1038/s41467-021-25635-y
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Zhiqiang Hou Pawel M. Wydorski Valerie A. Perez Aydé Mendoza-Oliva Bryan D. Ryder Hilda Mirbaha Omar Kashmer Lukasz A. Joachimiak
spellingShingle	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 Nature Communications
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 Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2021-09-01
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.
url	https://doi.org/10.1038/s41467-021-25635-y
work_keys_str_mv	AT zhiqianghou dnajc7bindsnativelyfoldedstructuralelementsintautoinhibitamyloidformation AT pawelmwydorski dnajc7bindsnativelyfoldedstructuralelementsintautoinhibitamyloidformation AT valerieaperez dnajc7bindsnativelyfoldedstructuralelementsintautoinhibitamyloidformation AT aydemendozaoliva dnajc7bindsnativelyfoldedstructuralelementsintautoinhibitamyloidformation AT bryandryder dnajc7bindsnativelyfoldedstructuralelementsintautoinhibitamyloidformation AT hildamirbaha dnajc7bindsnativelyfoldedstructuralelementsintautoinhibitamyloidformation AT omarkashmer dnajc7bindsnativelyfoldedstructuralelementsintautoinhibitamyloidformation AT lukaszajoachimiak dnajc7bindsnativelyfoldedstructuralelementsintautoinhibitamyloidformation
_version_	1717755429698666496

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

Similar Items