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TitlePhosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 6697, Year 2021
Publish dateNov 18, 2021
AuthorsMoritz Mühlhofer / Carsten Peters / Thomas Kriehuber / Marina Kreuzeder / Pamina Kazman / Natalia Rodina / Bernd Reif / Martin Haslbeck / Sevil Weinkauf / Johannes Buchner /
PubMed AbstractHsp26 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 ...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 conserved core domain of Hsp26 and the so-called thermosensor domain in the N-terminal part of the protein, which are targeted by phosphorylation. Furthermore, several phosphorylation sites in the C-terminal extension, which link subunits within the oligomer, are sensitive to the introduction of negative charges. In all cases, the intrinsic inhibition of chaperone activity is relieved and the N-terminal domain becomes accessible for substrate protein binding. The weakening of domain interactions within and between subunits by phosphorylation to activate the chaperone activity in response to proteotoxic stresses independent of heat stress could be a general regulation principle of sHsps.
External linksNat Commun / PubMed:34795272 / PubMed Central
MethodsEM (single particle)
Resolution7.8 - 16.45 Å
Structure data

12766

7oa6

EMDB-12766: Single particle cryo-EM reconstruction of just the top two rings of a 40-mer assembly of recombinant yeast Hsp26 S207E mutant.
PDB-7oa6: Pseudo-atomic model for Hsp26 residues 63 to 214. Please be advised that the target map is not of sufficient resolution to unambiguously position backbone or side chain atoms. This model represents a likely fit.
Method: EM (single particle) / Resolution: 7.8 Å

EMDB-12771:
Single particle cryo-EM reconstruction of a 40-mer assembly of recombinant yeast Hsp26 S207E mutant.
Method: EM (single particle) / Resolution: 8.76 Å

EMDB-12772:
Single particle cryo-EM reconstruction of a 40-mer assembly of recombinant yeast Hsp26 mutant S47ET48E.
Method: EM (single particle) / Resolution: 16.45 Å

EMDB-12773:
Single particle cryo-EM reconstruction of a 40-mer assembly of recombinant yeast Hsp26.
Method: EM (single particle) / Resolution: 9.6 Å

EMDB-13748:
Preliminary Single particle cryo-EM reconstruction of a 40-mer assembly of Hsp26 purified from yeast.
Method: EM (single particle) / Resolution: 10.0 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsCHAPERONE / small heat shock proteins / Hsp26 S207E mutant

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