A quantitative characterization of interaction between prion protein with nucleic acids

Biochemistry and Biophysics Reports

Sajal Biring¹  Alakesh Bera² 

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

关键词: Prion protein;    Small highly structured RNAs (shsRNAs);    Pseudoknots;    Poly A;    Fluorescence anisotropy (r);    Binding constant (Kd);   

DOI  :  10.1016/j.bbrep.2018.04.006

来源: DOAJ

【 摘 要 】

Binding of recombinant prion protein with small highly structured RNAs, prokaryotic and eukaryotic prion protein mRNA pseudoknots, tRNA and polyA has been studied by the change in fluorescence anisotropy of the intrinsic tryptophan groups of the protein. The affinities of these RNAs to the prion protein and the number of sites where the protein binds to the nucleic acids do not vary appreciably although the RNAs have very different compositions and structures. The binding parameters do not depend upon pH of the solution and show a poor co-operativity. The reactants form larger nucleoprotein complexes at pH 5 compared to that at neutral pH. The electrostatic force between the protein and nucleic acids dominates the binding interaction at neutral pH. In contrast, nucleic acid interaction with the incipient nonpolar groups exposed from the structured region of the prion protein dominates the reaction at pH 5. Prion protein of a particular species forms larger complexes with prion protein mRNA pseudoknots of the same species. The structure of the pseudoknots and not their base sequences probably dominates their interaction with prion protein. Possibilities of the conversion of the prion protein to its infectious form in the cytoplasm by nucleic acids have been discussed.

【 授权许可】

Unknown