Beta-synuclein exhibits chaperone activity more efficiently than alpha-synuclein.
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.
Division of Molecular and Life Sciences, National Research Laboratory of Protein Folding and Engineering, Pohang University of Science and Technology, Pohang 790-784, Republic of Korea.
Daekyun
D
Lee
Seung R
SR
Paik
Kwan Yong
KY
Choi
D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000037:antagonists & inhibitors; D002950:Citrate (si)-Synthase / Q000378:metabolism; D006358:Hot Temperature; D018832:Molecular Chaperones; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D051843:Synucleins; D051844:alpha-Synuclein; D051846:beta-Synuclein
D016229:Amyloid beta-Peptides; D018832:Molecular Chaperones; D009419:Nerve Tissue Proteins; D051843:Synucleins; D051844:alpha-Synuclein; D051846:beta-Synuclein; D002950:Citrate (si)-Synthase