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Article

Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble.

Nature communications - 18 Nov 2021

Mühlhofer Moritz, Peters Carsten, Kriehuber Thomas, Kreuzeder Marina, Kazman Pamina, Rodina Natalia, Reif Bernd, Haslbeck Martin, Weinkauf Sevil, Buchner Johannes

Abstract excerpt

Hsp26 is a small heat shock protein (sHsp) from S. cerevisiae. Its chaperone activity is activated by oligomer dissociation at heat shock temperatures. Hsp26 contains 9 phosphorylation sites in different structural elements. Our analysis of phospho-mimetic mutations shows that phosphorylation activates Hsp26 at permissive temperatures. The cryo-EM structure of the Hsp26 40mer revealed contacts between the...

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Identifiers

PMID: 34795272
DOI: 10.1038/s41467-021-27036-7
PMCID: PMC8602628

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