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DNA induced folding/fibrillation of alpha-synuclein: new insights in Parkinson's disease.

Muralidhar, L. Hegde and Padmaraju, Vasudevaraju and Jagannatha Rao, Kosagi Sharaf (2010) DNA induced folding/fibrillation of alpha-synuclein: new insights in Parkinson's disease. Frontiers in Bioscience-Landmark, 15. pp. 418-436.

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Emerging evidences on the nuclear localization of alpha-Synuclein in neurons and a close look in to its primary sequence/structural organization led us to examine its DNA binding ability. Subsequently, we first time demonstrated the interaction of DNA with alpha-Synuclein which was also confirmed by others. We recently showed that double-stranded oligos induce partial folding in alpha-Synuclein and promote its aggregation, where as single-strand circular DNA and supercoiled plasmid DNA induced a helix-rich conformation and protected the protein from fibrillation. In turn, alpha-Synuclein modulates DNA conformation from B- to an altered B-form, which may affect DNA transactions. Interestingly, amyloid-beta peptides and prion proteins implicated in Alzheimer's disease and Prion diseases respectively, were also shown to have DNA binding activity which suggests that DNA binding may be a common property of many amyloidogenic proteins associated with various neurodegenerative disorders. In this review, we debate the biological significance of DNA-alpha-Synuclein interactions; it's beneficial vs. toxic role in relevance to Parkinson's disease.

Item Type: Article
Uncontrolled Keywords: Oxidative stress ; DNA damage; Alzheimer's disease
Subjects: 600 Technology > 01 Medical sciences
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 03 Aug 2011 11:15
Last Modified: 04 Jun 2019 10:34
URI: http://ir.cftri.com/id/eprint/10387

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