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

Authors :
Zhiqiang Hou
Pawel M. Wydorski
Valerie A. Perez
Aydé Mendoza-Oliva
Bryan D. Ryder
Hilda Mirbaha
Omar Kashmer
Lukasz A. Joachimiak
Source :
Nature Communications, Vol 12, Iss 1, Pp 1-17 (2021)
Publication Year :
2021
Publisher :
Nature Portfolio, 2021.

Abstract

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.

Subjects

Subjects :
Science

Details

Language :
English
ISSN :
20411723
Volume :
12
Issue :
1
Database :
Directory of Open Access Journals
Journal :
Nature Communications
Publication Type :
Academic Journal
Accession number :
edsdoj.f2e4491eb9574af5a1fdc65f39a15797
Document Type :
article
Full Text :
https://doi.org/10.1038/s41467-021-25635-y