On the substrate specificity of alpha-crystallin as a molecular chaperone.
alpha-Crystallin, the major protein of the ocular lens, acts as a molecular chaperone by preventing the thermal aggregation of proteins. However, in contrast with many other heat shock proteins, alpha-crystallin fails to protect proteins from aggregation during refolding reactions. Our results indicate that alpha-crystallin has substrate specificity different from other chaperones and recognizes specific non-native intermediates formed on the denaturation pathway only, with no affinity for intermediates formed on the refolding pathway.
D000818:Animals; D002151:Calorimetry; D002417:Cattle; D018834:Chaperonin 60 / Q000378:metabolism; D002850:Chromatography, Gel; D003459:Crystallins / Q000302:isolation & purification / Q000378:metabolism*; D006358:Hot Temperature; D007908:Lens, Crystalline / Q000737:chemistry; D018832:Molecular Chaperones / Q000378:metabolism*; D011489:Protein Denaturation; D013379:Substrate Specificity; D013884:Thiosulfate Sulfurtransferase / Q000378:metabolism
D018834:Chaperonin 60; D003459:Crystallins; D018832:Molecular Chaperones; D013884:Thiosulfate Sulfurtransferase