Nature Communications (Sep 2021)

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

  • Zhiqiang Hou,
  • Pawel M. Wydorski,
  • Valerie A. Perez,
  • Aydé Mendoza-Oliva,
  • Bryan D. Ryder,
  • Hilda Mirbaha,
  • Omar Kashmer,
  • Lukasz A. Joachimiak

DOI
https://doi.org/10.1038/s41467-021-25635-y
Journal volume & issue
Vol. 12, no. 1
pp. 1 – 17

Abstract

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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.