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Fluorescence and nucleic acid binding properties of bovine leukemia virus nucleocapsid protein

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

  2. Author Address

    NCI, Frederick Canc Res & Dev Ctr, AIDS Vaccine Program, SAIC Frederick, Bldg 535,5th Floor,POB B, Frederick, MD 21702 USA NCI, Frederick Canc Res & Dev Ctr, AIDS Vaccine Program, SAIC Frederick, Frederick, MD 21702 USA Informax Inc, Bethesda, MD 20814 USA Medimmune Inc, Gaithersburg, MD 20878 USA Morcock DR NCI, Frederick Canc Res & Dev Ctr, AIDS Vaccine Program, SAIC Frederick, Bldg 535,5th Floor,POB B, Frederick, MD 21702 USA
    1. Year: 2002
  2. Journal: Biophysical Chemistry
    1. 97
    2. 2-3
    3. Pages: 203-212
  4. Type of Article: Article
  1. Abstract:

    We used the intrinsic fluorescence of bovine leukemia virus p12, a nucleocapsid protein with two tryptophan-containing zinc fingers (ZFs), to study its conformation and binding to single- stranded nucleic acids. Spectral emission maxima suggested solvent-exposed tryptophans. A peptide derived from ZF1 had a higher quantum yield and longer average lifetime (tau) than ZF2. BLV p12 tau and rotational correlation time were greater than ZF values, but all de-metallated sequences gave similar results. Apo p12 showed reduced fluorescence intensity, T and loss of secondary structure. DNA-binding affinity of p12 was in the nanomolar range, and decreased 14-fold after Zn++ ejection. Nucleobase preference of BLV p12 was different from the closely related HTLV-1 but similar to HIV-1 and SIV nucleocapsids, both phylogenetically distant. (C) 2002 Elsevier Science B.V All rights reserved.

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