Interactions of the DNA polymerase X from African Swine Fever Virus with the ssDNA. Properties of the total DNA-binding site and the strong DNA-binding subsite

Maria J. Jezewska, Michal R. Szymanski, Wlodzimierz Bujalowski

    Research output: Contribution to journalArticle

    3 Scopus citations

    Abstract

    Interactions of the polymerase X from the African Swine Fever Virus with the ssDNA have been studied, using quantitative fluorescence titration and fluorescence resonance energy transfer techniques. The primary DNA-binding subsite of the enzyme, independent of the DNA conformation, is located on the C-terminal domain. Association of the bound DNA with the catalytic N-terminal domain finalizes the engagement of the total DNA-binding site of the enzyme and induces a large topological change in the structure of the bound ssDNA. The free energy of binding includes a conformational transition of the protein. Large positive enthalpy changes accompanying the ASFV pol X-ssDNA association indicate that conformational changes of the complex are induced by the engagement of the N-terminal domain. The enthalpy changes are offset by large entropy changes accompanying the DNA binding to the C-terminal domain and the total DNA-binding site, predominantly resulting from the release of water molecules.

    Original languageEnglish (US)
    Pages (from-to)26-37
    Number of pages12
    JournalBiophysical Chemistry
    Volume158
    Issue number1
    DOIs
    StatePublished - Sep 1 2011

    Keywords

    • DNA replication
    • Fluorescence titrations
    • Motor protein
    • Polymerase
    • Protein-DNA interaction

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Organic Chemistry

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