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TitleRegulated structural transitions unleash the chaperone activity of αB-crystallin.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 110, Issue 40, Page E3780-E3789, Year 2013
Publish dateOct 1, 2013
AuthorsJirka Peschek / Nathalie Braun / Julia Rohrberg / Katrin Christiane Back / Thomas Kriehuber / Andreas Kastenmüller / Sevil Weinkauf / Johannes Buchner /
PubMed AbstractThe small heat shock protein αB-crystallin is an oligomeric molecular chaperone that binds aggregation-prone proteins. As a component of the proteostasis system, it is associated with cataract, ...The small heat shock protein αB-crystallin is an oligomeric molecular chaperone that binds aggregation-prone proteins. As a component of the proteostasis system, it is associated with cataract, neurodegenerative diseases, and myopathies. The structural determinants for the regulation of its chaperone function are still largely elusive. Combining different experimental approaches, we show that phosphorylation-induced destabilization of intersubunit interactions mediated by the N-terminal domain (NTD) results in the remodeling of the oligomer ensemble with an increase in smaller, activated species, predominantly 12-mers and 6-mers. Their 3D structures determined by cryo-electron microscopy and biochemical analyses reveal that the NTD in these species gains flexibility and solvent accessibility. These modulated properties are accompanied by an increase in chaperone activity in vivo and in vitro and a more efficient cooperation with the heat shock protein 70 system in client folding. Thus, the modulation of the structural flexibility of the NTD, as described here for phosphorylation, appears to regulate the chaperone activity of αB-crystallin rendering the NTD a conformational sensor for nonnative proteins.
External linksProc Natl Acad Sci U S A / PubMed:24043785 / PubMed Central
MethodsEM (single particle)
Resolution17.0 Å
Structure data

EMDB-2366:
Electron cryo-microscopy of phosphorylation-mimicking mutants of alphaB-crystallin: the hexamer
Method: EM (single particle) / Resolution: 17.0 Å

Source
  • Homo sapiens (human)

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