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Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism.

Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism. Research Abstract Details 

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  • Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism. Abstract Text:

    arianna loregianArianna Loregian,elisa sinigaliaElisa Sinigalia,beatrice mercorelliBeatrice Mercorelli,giorgio Giorgio ,donald m coenDonald M Coen,

    The mechanisms of processivity factors of herpesvirus DNA polymerases remain poorly understood. The proposed processivity factor for human cytomegalovirus DNA polymerase is a DNA-binding protein, UL44. Previous findings, including the crystal structure of UL44, have led to the hypothesis that UL44 binds DNA as a dimer via lysine residues. To understand how UL44 interacts with DNA, we used filter-binding and electrophoretic mobility shift assays and isothermal titration calorimetry (ITC) analysis of binding to oligonucleotides. UL44 bound directly to double-stranded DNA as short as 12 bp, with apparent dissociation constants in the nanomolar range for DNAs >18 bp, suggesting a minimum DNA length for UL44 interaction. UL44 also bound single-stranded DNA, albeit with lower affinity, and for either single- or double-stranded DNA, there was no apparent sequence specificity. ITC analysis revealed that UL44 binds to duplex DNA as a dimer. Binding was endothermic, indicating an entropically driven process, likely due to release of bound ions. Consistent with this hypothesis, analysis of the relationship between binding and ionic strength indicated that, on average, 4 +/- 1 monovalent ions are released in the interaction of each monomer of UL44 with DNA. The results taken together reveal interesting implications for how UL44 may mediate processivity.

    Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism. Publishing Authors By Initials

    a loregianA Loregian,e sinigaliaE Sinigalia,b mercorelliB Mercorelli,g G ,dm coenDM Coen,

    For similar proteins: viral proteins research abstracts see: proteins: viral proteins research

    PUBMED ID PMID:

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    Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Nucleic acids research

    VOLUME: 35

    Page Numbers: 4779-91

    Journal Abbreviation: Nucleic Acids Res.

    ISSN: 1362-4962

    DAY: 7

    MONTH: 07

    YEAR: 2007

    Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 411011

    Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism. Keywords Mesh Terms:

    KEYWORDS: Viral Proteins

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism. Information

    Substance Name: DNA

    Registry Number: 9007-49-2

    Grant and Affiliation Information for Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism.

    AFFILIATION: Department of Histology, Microbiology and Medical Biotechnologies, University of Padova, 35121 Padova, Italy. arianna.loregian@unipd.it

    Country: England

    England Research PublicationEngland Research Publication

    AGENCY: United States NIAID

    GRANT: AI19838

    ACRONYM: AI

    MEDLINETA: Nucleic Acids Res

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    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

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