CSIR Central

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

IR@CFTRI: CSIR-Central Food Technological Research Institute, Mysore


Field	Value

Relation	http://ir.cftri.com/10387/ FB-01-10

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

Creator	Muralidhar, L. Hegde Padmaraju, Vasudevaraju Jagannatha Rao, Kosagi Sharaf

Subject	01 Medical sciences

Description	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.

Date	2010

Type	Article PeerReviewed

Format	pdf

Language	en

Identifier	http://ir.cftri.com/10387/1/frontierinbioscience.pdf 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.