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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Autores principales: Rishav Mitra, Varun V. Gadkari, Ben A. Meinen, Carlo P. M. van Mierlo, Brandon T. Ruotolo, James C. A. Bardwell
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/faf6241cffc94273ba8452b252a93b6d
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Sumario: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.