| http://purl.uniprot.org/citations/20937351 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20937351 | http://www.w3.org/2000/01/rdf-schema#comment | "δ-Crystallin is a taxon-specific eye lens protein that was recruited from argininosuccinate lyase (ASL) through gene sharing. ASL is a metabolic enzyme that catalyzes the reversible conversion of argininosuccinate into arginine and fumarate and shares about 70% sequence identity and similar overall topology with δ-crystallin. ASL has a lower thermal stability than δ-crystallin. In this study, we show that the small heat shock protein, αA-crystallin, functions as a molecular chaperone, and enhanced thermal stability of both δ-crystallin and ASL. The stoichiometry for efficient protection of the two substrate proteins by αA-crystallin was determined by slowly increasing the temperature. N- or C-terminal truncated mutants of δ-crystallin co-incubated with αA-crystallin showed higher thermal stability than wild-type enzyme, and the stoichiometry for efficient protection was the same. Thermal unfolding of δ-crystallin or ASL in the presence of αA-crystallin followed a similar three-state model, as determined by circular dichroism analyses. A stable intermediate which retained about 30% α-helical structure was observed. Protection from thermal denaturation by αA-crystallin was by interaction with partly unfolded ASL or δ-crystallin to form high molecular weight heteroligomers, as judged by size-exclusive chromatography and SDS-PAGE analyses. Aggregate formation of ASL was significantly reduced in the presence of αA-crystallin. The extent of protection of ASL and δ-crystallin at different ratios of αA-crystallin were described by hyperbolic and sigmoidal curves, respectively. These results suggest the preferential recognition of partly unfolded ASL by αA-crystallin. In contrast, unstable δ-crystallin might trigger a cooperative interaction by higher stoichiometries of αA-crystallin leading to fuller protection. The different interactions of αA-crystallin with the two homologous but functionally different substrate proteins show its behavior as a chaperone is variable."xsd:string |
| http://purl.uniprot.org/citations/20937351 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.biochi.2010.10.003"xsd:string |
| http://purl.uniprot.org/citations/20937351 | http://purl.uniprot.org/core/author | "Chen Y.H."xsd:string |
| http://purl.uniprot.org/citations/20937351 | http://purl.uniprot.org/core/author | "Lee H.J."xsd:string |
| http://purl.uniprot.org/citations/20937351 | http://purl.uniprot.org/core/author | "Lee M.T."xsd:string |
| http://purl.uniprot.org/citations/20937351 | http://purl.uniprot.org/core/author | "Chou W.Y."xsd:string |
| http://purl.uniprot.org/citations/20937351 | http://purl.uniprot.org/core/author | "Yu C.M."xsd:string |
| http://purl.uniprot.org/citations/20937351 | http://purl.uniprot.org/core/author | "Cheng Y.W."xsd:string |
| http://purl.uniprot.org/citations/20937351 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/20937351 | http://purl.uniprot.org/core/name | "Biochimie"xsd:string |
| http://purl.uniprot.org/citations/20937351 | http://purl.uniprot.org/core/pages | "314-320"xsd:string |
| http://purl.uniprot.org/citations/20937351 | http://purl.uniprot.org/core/title | "Distinct interactions of alphaA-crystallin with homologous substrate proteins, delta-crystallin and argininosuccinate lyase, under thermal stress."xsd:string |
| http://purl.uniprot.org/citations/20937351 | http://purl.uniprot.org/core/volume | "93"xsd:string |
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