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• W2110336102 endingPage "10452" @default.
• W2110336102 startingPage "10449" @default.
• W2110336102 abstract "α-Crystallin, the major protein of the ocular lens, acts as a molecular chaperone by suppressing the nonspecific aggregation of damaged proteins. To investigate the mechanism of the interaction between α-crystallin and substrate proteins, we prepared a tryptophan-free mutant of human αA-crystallin and assessed the conformation of thermally destabilized proteins captured by this chaperone using fluorescence spectroscopy. The fluorescence emission characteristics of bound substrates (rhodanese and γ-crystallin) and the results of fluorescence quenching experiments indicate that the proteins captured by α-crystallin are characterized by a very low degree of unfolding. In particular, the structure of rhodanese bound to αA-crystallin appears to be considerably more native-like compared to that of the enzyme bound to the chaperonin GroEL. We postulate that α-crystallin (and likely other small heat shock proteins) recognize preferentially the aggregation-prone conformers that occur very early on the denaturation pathway. With its ability to capture and stabilize these early non-native structures, α-crystallin appears to be uniquely well suited to chaperone the transparency properties of the ocular lens. α-Crystallin, the major protein of the ocular lens, acts as a molecular chaperone by suppressing the nonspecific aggregation of damaged proteins. To investigate the mechanism of the interaction between α-crystallin and substrate proteins, we prepared a tryptophan-free mutant of human αA-crystallin and assessed the conformation of thermally destabilized proteins captured by this chaperone using fluorescence spectroscopy. The fluorescence emission characteristics of bound substrates (rhodanese and γ-crystallin) and the results of fluorescence quenching experiments indicate that the proteins captured by α-crystallin are characterized by a very low degree of unfolding. In particular, the structure of rhodanese bound to αA-crystallin appears to be considerably more native-like compared to that of the enzyme bound to the chaperonin GroEL. We postulate that α-crystallin (and likely other small heat shock proteins) recognize preferentially the aggregation-prone conformers that occur very early on the denaturation pathway. With its ability to capture and stabilize these early non-native structures, α-crystallin appears to be uniquely well suited to chaperone the transparency properties of the ocular lens." @default.
• W2110336102 created "2016-06-24" @default.
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• W2110336102 date "1996-05-01" @default.
• W2110336102 modified "2023-10-16" @default.
• W2110336102 title "Conformational Properties of Substrate Proteins Bound to a Molecular Chaperone α-Crystallin" @default.
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• W2110336102 doi "https://doi.org/10.1074/jbc.271.18.10449" @default.
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