The eye lens chaperone alpha-crystallin forms defined globular assemblies.
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.
Peschek
Jirka
J
Center for Integrated Protein Science and Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching, Germany.
Braun
Nathalie
N
Franzmann
Titus M
TM
Georgalis
Yannis
Y
Haslbeck
Martin
M
Weinkauf
Sevil
S
Buchner
Johannes
J
D000818:Animals; D002417:Cattle; D006801:Humans; D007908:Lens, Crystalline / Q000737:chemistry*; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D038201:alpha-Crystallins / Q000737:chemistry* / Q000648:ultrastructure
D038201:alpha-Crystallins