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Proc Natl Acad Sci U S A. 2009 Aug 11;106(32):13272-7. doi: 10.1073/pnas.0902651106. Epub 2009 Jul 27.

The eye lens chaperone alpha-crystallin forms defined globular assemblies.

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  • 1Center for Integrated Protein Science and Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching, Germany.

Abstract

Alpha-crystallins are molecular chaperones that protect vertebrate eye lens proteins from detrimental protein aggregation. alphaB-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 alphaB-crystallin assembles into defined oligomers consisting of 24 subunits. The 3-dimensional (3D) reconstruction of alphaB-crystallin by electron microscopy reveals a sphere-like structure with large openings to the interior of the protein. alphaA-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.

PMID:
19651604
[PubMed - indexed for MEDLINE]
PMCID:
PMC2726422
Free PMC Article
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