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Role of the histidine residues of visna virus nucleocapsid protein in metal ion and DNA binding

  1. Author:
    Morcock, D. R.
    Sowder, R. C.
    Casas-Finet, J. R.

  2. Author Address

    Casas-Finet JR NCI, AIDS Vaccine Program, SAIC Frederick, Frederick Canc Res & Dev Ctr Bldg 535-4,POB B Frederick, MD 21702 USA NCI, AIDS Vaccine Program, SAIC Frederick, Frederick Canc Res & Dev Ctr Frederick, MD 21702 USA
    1. Year: 2000
  2. Journal: Febs Letters
    1. 476
    2. 3
    3. Pages: 190-193
  4. Type of Article: Article
  1. Abstract:

    Zinc finger (ZF) domains in retroviral nucleocapsid proteins usually contain one histidine per metal ion coordination complex (Cys-X-2-Cys-X-4-His-X-4-Cys). Visna virus nucleocapsid protein, p8, has two additional histidines (in the second of its two ZFs) that could potentially bind metal ions. Absorption spectra of cobalt-bound ZF2 peptides were altered by Cys alkylation and mutation, but not by mutation of the extra histidines. Our results show that visna p8 ZFs involve three Cys and one His in the canonical spacing in metal ion coordination, and that the two additional histidines appear to interact with nucleic acid bases in p8-DNA complexes. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved. [References: 16]

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