Beta-synuclein exhibits chaperone activity more efficiently than alpha-synuclein.

Daekyun Lee; Seung R Paik; Kwan Yong Choi

doi:10.1016/j.febslet.2004.08.075

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Beta-synuclein exhibits chaperone activity more efficiently than alpha-synuclein.

Daekyun Lee·Seung R Paik·Kwan Yong Choi

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Abstract

Beta-synuclein exhibits high sequence homology and structural similarity with alpha-synuclein, a protein implicated in the pathogenesis of Parkinson's disease. We investigated the chaperone function of beta-synuclein and its anti-fibrillar activity in comparison with alpha-synuclein. beta-Synuclein suppressed the heat-induced aggregation of aldolase, alcohol dehydrogenase, and citrate synthase, and its anti-aggregative activity was remarkably higher than that of alpha-synuclein. Heat-induced inactivation of citrate synthase was significantly protected by beta-synuclein. Moreover, beta-synuclein inhibited the amyloid formation of both Abeta(1-40) and alpha-synuclein. It is, therefore, suggested that beta-synuclein can prevent abnormal protein aggregations more effectively than alpha-synuclein by acting as a molecular chaperone.

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Amino Acid Sequence Amyloid beta-Peptides Citrate (si)-Synthase Hot Temperature Molecular Chaperones Molecular Sequence Data Nerve Tissue Proteins Sequence Homology, Amino Acid Synucleins alpha-Synuclein beta-Synuclein Comparative Study Journal Article Research Support, Non-U.S. Gov't

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Daekyun Lee, Seung R Paik, Kwan Yong Choi. 2004-10-08. Beta-synuclein exhibits chaperone activity more efficiently than alpha-synuclein.. https://doi.org/10.1016/j.febslet.2004.08.075

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