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
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/faf6241cffc94273ba8452b252a93b6d
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spelling	oai:doaj.org-article:faf6241cffc94273ba8452b252a93b6d2021-12-02T14:26:51ZMechanism of the small ATP-independent chaperone Spy is substrate specific10.1038/s41467-021-21120-82041-1723https://doaj.org/article/faf6241cffc94273ba8452b252a93b6d2021-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21120-8https://doaj.org/toc/2041-1723Spy 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.Rishav MitraVarun V. GadkariBen A. MeinenCarlo P. M. van MierloBrandon T. RuotoloJames C. A. BardwellNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Rishav Mitra Varun V. Gadkari Ben A. Meinen Carlo P. M. van Mierlo Brandon T. Ruotolo James C. A. Bardwell Mechanism of the small ATP-independent chaperone Spy is substrate specific
description	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.
format	article
author	Rishav Mitra Varun V. Gadkari Ben A. Meinen Carlo P. M. van Mierlo Brandon T. Ruotolo James C. A. Bardwell
author_facet	Rishav Mitra Varun V. Gadkari Ben A. Meinen Carlo P. M. van Mierlo Brandon T. Ruotolo James C. A. Bardwell
author_sort	Rishav Mitra
title	Mechanism of the small ATP-independent chaperone Spy is substrate specific
title_short	Mechanism of the small ATP-independent chaperone Spy is substrate specific
title_full	Mechanism of the small ATP-independent chaperone Spy is substrate specific
title_fullStr	Mechanism of the small ATP-independent chaperone Spy is substrate specific
title_full_unstemmed	Mechanism of the small ATP-independent chaperone Spy is substrate specific
title_sort	mechanism of the small atp-independent chaperone spy is substrate specific
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/faf6241cffc94273ba8452b252a93b6d
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Mechanism of the small ATP-independent chaperone Spy is substrate specific

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