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Complex interactions of HIV-1 nucleocapsid protein with oligonucleotides

  1. Author:
    Fisher, R. J.
    Fivash, M. J.
    Stephen, A. G.
    Hagan, N. A.
    Shenoy, S. R.
    Medaglia, M. V.
    Smith, L. R.
    Worthy, K. M.
    Simpson, J. T.
    Shoemaker, R.
    McNitt, K. L.
    Johnson, D. G.
    Hixson, C. V.
    Gorelick, R. J.
    Fabris, D.
    Henderson, L. E.
    Rein, A.

  2. Author Address

    NCI, Prot Chem Lab, SAIC Frederick Inc, Frederick, MD 21702 USA. NCI, Data Management Serv Inc, Frederick, MD 21702 USA. Univ Maryland Baltimore Cty, Dept Chem & Biochem, Baltimore, MD 21250 USA. NCI, Mol Targets Dev Program, Basic Res Program, SAIC Frederick Inc, Frederick, MD 21702 USA. NCI, Screening Technol Branch, Dev Therapeut Program, Div Canc Treatment & Diag, Frederick, MD 21702 USA. NCI, AIDS Vaccine Program, SAIC Frederick Inc, Frederick, MD 21702 USA. NCI, HIV Drug Resistance Program, Frederick, MD 21702 USA Fisher, RJ, NCI, Prot Chem Lab, SAIC Frederick Inc, Frederick, MD 21702 USA
    1. Year: 2006
  2. Journal: Nucleic Acids Research
    1. 34
    2. 2
    3. Pages: 472-484
  4. Type of Article: Article
  1. Abstract:

    The HIV-1 nucleocapsid (NC) protein is a small, basic protein containing two retroviral zinc fingers. It is a highly active nucleic acid chaperone; because of this activity, it plays a crucial role in virus replication as a cofactor during reverse transcription, and is probably important in other steps of the replication cycle as well. We previously reported that NC binds with high-affinity to the repeating sequence d(TG)(n). We have now analyzed the interaction between NC and d(TG)(4) in considerable detail, using surface plasmon resonance (SPR), tryptophan fluorescence quenching (TFQ), fluorescence anisotropy (FA), isothermal titration calorimetry (ITC) and electrospray ionization Fourier transform mass spectrometry (ESI-FTMS). Our results show that the interactions between these two molecules are surprisngly complex: while the K-d for binding of a single d(TG)(4) molecule to NC is only similar to 5 nM in 150 mM NaCl, a single NC molecule is capable of interacting with more than one d(TG)(4) molecule, and conversely, more than one NC molecule can bind to a single d(TG)(4) molecule. The strengths of these additional binding reactions are quantitated. The implications of this multivalency for the functions of NC in virus replication are discussed

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  2. WOS: 000235291300018

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