Mechanism of the small ATP-independent chaperone Spy is substrate specific

Mechanism of the small ATP-independent chaperone Spy is substrate specific

Spy is an ATP independent chaperone that can act as both a holdase and a foldase towards topologically simple substrates. Assessing the interaction of Spy and apoflavodoxin, a complex client, the authors show that Spy’s activity is substrate specific. Spy binds partially unfolded states of apoflavod...

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Bibliographic Details
Main Authors: Rishav Mitra, Varun V. Gadkari, Ben A. Meinen, Carlo P. M. van Mierlo, Brandon T. Ruotolo, James C. A. Bardwell
Format: Article
Language:English
Published: Nature Publishing Group 2021-02-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-21120-8
Description
Summary:Spy is an ATP independent chaperone that can act as both a holdase and a foldase towards topologically simple substrates. Assessing the interaction of Spy and apoflavodoxin, a complex client, the authors show that Spy’s activity is substrate specific. Spy binds partially unfolded states of apoflavodoxin tightly, which limits the possibility of folding and converts Spy to a pure holdase.
ISSN:2041-1723

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