The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range

S. cerevisiae encodes two Hsp90 isoforms, the constitutively expressed Hsc82 and stress-inducible Hsp82 that are 97% identical. Here, the authors combine a range of biophysical methods and show that they differ in their enzymatic properties, resilience to stress and client range, which suggests that...

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Autores principales:	Hannah Girstmair, Franziska Tippel, Abraham Lopez, Katarzyna Tych, Frank Stein, Per Haberkant, Philipp Werner Norbert Schmid, Dominic Helm, Matthias Rief, Michael Sattler, Johannes Buchner
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/99faff43afb1456f9d5206c5879c275f
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spelling	oai:doaj.org-article:99faff43afb1456f9d5206c5879c275f2021-12-02T15:35:16ZThe Hsp90 isoforms from S. cerevisiae differ in structure, function and client range10.1038/s41467-019-11518-w2041-1723https://doaj.org/article/99faff43afb1456f9d5206c5879c275f2019-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11518-whttps://doaj.org/toc/2041-1723S. cerevisiae encodes two Hsp90 isoforms, the constitutively expressed Hsc82 and stress-inducible Hsp82 that are 97% identical. Here, the authors combine a range of biophysical methods and show that they differ in their enzymatic properties, resilience to stress and client range, which suggests that they evolved to provide fine-tuned chaperone assistance under physiological and stress conditions.Hannah GirstmairFranziska TippelAbraham LopezKatarzyna TychFrank SteinPer HaberkantPhilipp Werner Norbert SchmidDominic HelmMatthias RiefMichael SattlerJohannes BuchnerNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Hannah Girstmair Franziska Tippel Abraham Lopez Katarzyna Tych Frank Stein Per Haberkant Philipp Werner Norbert Schmid Dominic Helm Matthias Rief Michael Sattler Johannes Buchner The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range
description	S. cerevisiae encodes two Hsp90 isoforms, the constitutively expressed Hsc82 and stress-inducible Hsp82 that are 97% identical. Here, the authors combine a range of biophysical methods and show that they differ in their enzymatic properties, resilience to stress and client range, which suggests that they evolved to provide fine-tuned chaperone assistance under physiological and stress conditions.
format	article
author	Hannah Girstmair Franziska Tippel Abraham Lopez Katarzyna Tych Frank Stein Per Haberkant Philipp Werner Norbert Schmid Dominic Helm Matthias Rief Michael Sattler Johannes Buchner
author_facet	Hannah Girstmair Franziska Tippel Abraham Lopez Katarzyna Tych Frank Stein Per Haberkant Philipp Werner Norbert Schmid Dominic Helm Matthias Rief Michael Sattler Johannes Buchner
author_sort	Hannah Girstmair
title	The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range
title_short	The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range
title_full	The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range
title_fullStr	The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range
title_full_unstemmed	The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range
title_sort	hsp90 isoforms from s. cerevisiae differ in structure, function and client range
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/99faff43afb1456f9d5206c5879c275f
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The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range

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