Journal
BIOPHYSICAL CHEMISTRY
Volume 141, Issue 2-3, Pages 135-139Publisher
ELSEVIER
DOI: 10.1016/j.bpc.2008.12.011
Keywords
Prion; DNA; Stability; Unfolding; pH; Urea; Guanidine hydrochloride
Funding
- Coordenacao Aperfeicoamento de Pessoal de Nivel Superior (CAPES)
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
- Millenium Institute for Structural Biology in Biomedicine and Biotechnology
- Fundaqao Carlos Chagas Filho de Amparo a Pesquisa do Estado do Rio de Janeiro (FAPERJ)
- Programa de Nucleos de Excelencia (PRONEX)
- Fundacao Universitdria Jose Bonifacio
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The prion protein (PrP) is the major agent involved in the transmissible spongiform encephalopathies (TSEs). Nucleic acids have been reported to bind PrP with high affinity, although the physiopathological roles for recognition are still not clear. In this work we investigate the stability of a soluble, 1:1 complex formed between an 18 base-pair DNA fragment and the full-length murine recombinant prion protein (mrPrP). DNA confers a gain in mrPrP stability against urea and guanidinium denaturation, which is enhanced at lower pHs and in moderate concentrations of NaCl. We discuss the cooperative folding transition coupled to DNA binding and acidification in terms of the possible cellular scenarios found during complex internalization and degradation. (C) 2009 Elsevier B.V. All rights reserved.
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