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    Biochemistry. 2008 Dec 23;47(51):13604-9.

    Alpha-Synuclein conformation affects its tyrosine-dependent oxidative aggregation.

    Ruf RA, Lutz EA, Zigoneanu IG, Pielak GJ.

    Source

    Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599, USA.

    Abstract

    Oxidative stress and aggregation of the protein alpha-synuclein are thought to be key factors in Parkinson's disease. Previous work shows that cytochrome c with H(2)O(2) causes tyrosine-dependent in vitro peroxidative aggregation of proteins, including alpha-synuclein. Here, we examine the role of each of alpha-synuclein's four tyrosine residues and how the protein's conformation affects covalent oxidative aggregation. When alpha-synuclein adopts a collapsed conformation, tyrosine 39 is essential for wild-type-like covalent aggregation. This lone N-terminal tyrosine, however, is not required for wild-type-like covalent aggregation in the presence of a denaturant or when alpha-synuclein is present in noncovalent fibrils. We also show that preformed oxidative aggregates are not incorporated into noncovalent fibrils. These data provide insight into how dityrosine may be formed in Lewy bodies seen in Parkinson's disease.

    PMID:
    19049426
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC2645542
    Free PMC Article

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