Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 106, Issue 32, Pages 13272-13277Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0902651106
Keywords
electron microscopy; molecular chaperone; protein aggregation; small heat shock protein; stress response
Categories
Funding
- Deutsche Forschungsgemeinschaft [SFB594]
- Fonds der chemischen Industrie
- Studienstiftung des deutschen Volkes
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alpha-Crystallins are molecular chaperones that protect vertebrate eye lens proteins from detrimental protein aggregation. alpha B-Crystallin, 1 of the 2 alpha-crystallin isoforms, is also associated with myopathies and neuropathological diseases. Despite the importance of alpha-crystallins in protein homeostasis, only little is known about their quaternary structures because of their seemingly polydisperse nature. Here, we analyzed the structures of recombinant alpha-crystallins using biophysical methods. In contrast to previous reports, we show that alpha B-crystallin assembles into defined oligomers consisting of 24 subunits. The 3-dimensional (3D) reconstruction of alpha B-crystallin by electron microscopy reveals a sphere-like structure with large openings to the interior of the protein. alpha A-Crystallin forms, in addition to complexes of 24 subunits, also smaller oligomers and large clusters consisting of individual oligomers. This propensity might explain the previously reported polydisperse nature of alpha-crystallin.
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