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Journal of Nucleic Acids
Volume 2018, Article ID 9581021, 14 pages
Research Article

A Sequence-Dependent DNA Condensation Induced by Prion Protein

1Infectiologie Animale et Santé Publique, Institut National de la Recherche Agronomique, 37380 Nouzilly, France
2Department of Electronic Engineering and Organic Electronics Research Center, Ming-Chi University of Technology, 84 Gungjuan Rd., Taishan Dist., New Taipei City 24301, Taiwan

Correspondence should be addressed to Alakesh Bera; ude.shusu@rtc.areb.hsekala and Sajal Biring; wt.ude.tucm.liam@gnirib

Received 18 October 2017; Revised 18 December 2017; Accepted 17 January 2018; Published 20 February 2018

Academic Editor: Ben Berkhout

Copyright © 2018 Alakesh Bera and Sajal Biring. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Different studies indicated that the prion protein induces hybridization of complementary DNA strands. Cell culture studies showed that the scrapie isoform of prion protein remained bound with the chromosome. In present work, we used an oxazole dye, YOYO, as a reporter to quantitative characterization of the DNA condensation by prion protein. We observe that the prion protein induces greater fluorescence quenching of YOYO intercalated in DNA containing only GC bases compared to the DNA containing four bases whereas the effect of dye bound to DNA containing only AT bases is marginal. DNA-condensing biological polyamines are less effective than prion protein in quenching of DNA-bound YOYO fluorescence. The prion protein induces marginal quenching of fluorescence of the dye bound to oligonucleotides, which are resistant to condensation. The ultrastructural studies with electron microscope also validate the biophysical data. The GC bases of the target DNA are probably responsible for increased condensation in the presence of prion protein. To our knowledge, this is the first report of a human cellular protein inducing a sequence-dependent DNA condensation. The increased condensation of GC-rich DNA by prion protein may suggest a biological function of the prion protein and a role in its pathogenesis.