Molten-Globule State of Carbonic Anhydrase Binds to the Chaperone-like α-Crystallin

α-Crystallin, a multimeric protein, exhibits chaperone-like activity in preventing aggregation of several proteins. We have studied the chaperone-like activity of α-crystallin toward heat-induced aggregation of bovine and human carbonic anhydrase. Human carbonic anhydrase aggregates at 60°C, while b...

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Veröffentlicht in:The Journal of biological chemistry 1996-11, Vol.271 (44), p.27595-27600
Hauptverfasser: Rajaraman, Krishnan, Raman, Bakthisaran, Rao, Ch. Mohan
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Sprache:eng
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Zusammenfassung:α-Crystallin, a multimeric protein, exhibits chaperone-like activity in preventing aggregation of several proteins. We have studied the chaperone-like activity of α-crystallin toward heat-induced aggregation of bovine and human carbonic anhydrase. Human carbonic anhydrase aggregates at 60°C, while bovine carbonic anhydrase does not aggregate significantly at this temperature. Removal of the enzyme-bound metal ion, Zn2+, by EDTA modulates the aggregation behavior of bovine carbonic anhydrase. Fluorescence and circular dichroism studies show that removal of the metal ion from the bovine carbonic anhydrase by a chelator such as EDTA enhances the propensity of the enzyme to adopt the molten-globule state. α-Crystallin binds to this state of the enzyme and prevents aggregation. Fluorescence and circular dichroism studies on the α-crystallin-enzyme complexes show that the enzymes in the complex are in the molten-globule state. These results are of relevance to the interaction of chaperones with the partially unfolded states of target proteins.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.271.44.27595