Insights into the client protein release mechanism of the ATP-independent chaperone Spy

Insights into the client protein release mechanism of the ATP-independent chaperone Spy

How ATP-independent chaperones release their clients without energy input remains enigmatic. Here the authors discover that chaperone Spy uses its long, disordered N terminus to facilitate client release through competitive, dynamic intramolecular interactions with Spy’s client binding surface.

Bibliographic Details
Main Authors: Wei He, Xinming Li, Hongjuan Xue, Yuanyuan Yang, Jun Mencius, Ling Bai, Jiayin Zhang, Jianhe Xu, Bin Wu, Yi Xue, Shu Quan
Format: Article
Language:English
Published: Nature Portfolio 2022-05-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-022-30499-x

Internet

https://doi.org/10.1038/s41467-022-30499-x

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