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


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.

SUBMITTER: Peschek J 

PROVIDER: S-EPMC2726422 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature

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

Peschek Jirka J   Braun Nathalie N   Franzmann Titus M TM   Georgalis Yannis Y   Haslbeck Martin M   Weinkauf Sevil S   Buchner Johannes J  

Proceedings of the National Academy of Sciences of the United States of America 20090727 32


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 biophysica  ...[more]

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