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Kaiser, C.J.O.* ; Peters, C.* ; Schmid, P.W.N.* ; Stavropoulou, M. ; Zou, J.* ; Dahiya, V.* ; Mymrikov, E.V.* ; Rockel, B.* ; Asami, S. ; Haslbeck, M.* ; Rappsilber, J.* ; Reif, B. ; Zacharias, M.* ; Buchner, J.* ; Weinkauf, S.*

The structure and oxidation of the eye lens chaperone αA-crystallin.

Nat. Struct. Mol. Biol. 26, 1141-1150 (2019)

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The small heat shock protein αA-crystallin is a molecular chaperone important for the optical properties of the vertebrate eye lens. It forms heterogeneous oligomeric ensembles. We determined the structures of human αA-crystallin oligomers by combining cryo-electron microscopy, cross-linking/mass spectrometry, NMR spectroscopy and molecular modeling. The different oligomers can be interconverted by the addition or subtraction of tetramers, leading to mainly 12-, 16- and 20-meric assemblies in which interactions between N-terminal regions are important. Cross-dimer domain-swapping of the C-terminal region is a determinant of αA-crystallin heterogeneity. Human αA-crystallin contains two cysteines, which can form an intramolecular disulfide in vivo. Oxidation in vitro requires conformational changes and oligomer dissociation. The oxidized oligomers, which are larger than reduced αA-crystallin and destabilized against unfolding, are active chaperones and can transfer the disulfide to destabilized substrate proteins. The insight into the structure and function of αA-crystallin provides a basis for understanding its role in the eye lens.

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