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Fluorescence and nucleic acid binding properties of the human T-cell leukemia virus-type 1 nucleocapsid protein

  1. Author:
    Morcock, D. R.
    Kane, B. P.
    Casas-Finet, J. R.

  2. Author Address

    NCI, Frederick Canc Res & Dev Ctr, AIDS Vaccine Program, SAIC Frederick, Bldg 535, 4th Floor, POB B, Frederick, MD 21702 USA. NCI, Frederick Canc Res & Dev Ctr, AIDS Vaccine Program, SAIC Frederick, Frederick, MD 21702 USA.
    1. Year: 2000
  2. Journal: Biochimica Et Biophysica Acta-Protein Structure and Molecular Enzymology
    1. 1481
    2. 2
    3. Pages: 381-394
  4. Type of Article: Article
  1. Abstract:

    We used intrinsic tryptophan fluorescence to study the nucleocapsid protein from human T-cell leukemia virus-type one, HTLV-1 p15, an 85-amino-acid protein with two Trp-containing zinc-finger motifs. Fluorescence spectra suggested an interaction between the two zinc fingers and another interaction involving the C-terminal tail and the zinc fingers. Titrations with nucleic acid revealed similar, sub-micromolar affinity for poly(dT) and poly(U) in 1 mM sodium phosphate, pH 7. Double-stranded DNA bound an order of magnitude weaker, suggesting helix-destabilizing activity. Base preference of p15 was T approximate to U>I approximate to C approximate to G>A; affinity spanned about one order of magnitude. HTLV-1 p15 bound weaker and with less variation than reported values for either human or simian immunodeficiency virus homologues. The low affinity of p15 for nonspecific nucleic acids distinguishes it from other nucleocapsid proteins, and may suggest its involvement in additional steps of the virus life cycle other than RNA packaging. (C) 2000 Elsevier Science B.V. All rights reserved.

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