       Document 0544
 DOCN  M9640544
 TI    Characterization of the DNA-binding activity of HIV-1 integrase using a
       filter binding assay.
 DT    9604
 AU    Haugan IR; Nilsen BM; Worland S; Olsen L; Helland DE; Laboratory of
       Biotechnology, University of Bergen, Norway.
 SO    Biochem Biophys Res Commun. 1995 Dec 26;217(3):802-10. Unique Identifier
       : AIDSLINE MED/96125314
 AB    Based on the selective binding of proteins and DNA to distinct filter
       materials a double-layered dot blot radio assay was developed to
       evaluate the binding of DNA to HIV-1 integrase. In this assay the
       DNA-binding was found to be independent of Mn2+ concentration, inhibited
       by concentrations of Mg2+ above 5 mM, abolished by zinc chelation and
       inhibited by monoclonal antibodies reacting with either the N-terminal
       or C-terminal regions of integrase. Atomic absorption spectroscopy
       revealed the molar ratio between integrase and zinc to be close to 1. It
       is concluded that both the N-terminal and the C-terminal regions of
       integrase are involved in DNA-binding and that the reported
       double-layered dot blot radio assay is well suited for further
       characterization of the integrase.
 DE    Base Sequence  DNA-Binding Proteins/*METABOLISM
       Endodeoxyribonucleases/*METABOLISM  HIV-1/*ENZYMOLOGY  Macromolecular
       Systems  Molecular Sequence Data  Oligodeoxyribonucleotides/CHEMISTRY
       Support, U.S. Gov't, P.H.S.  *Virus Integration  Zinc/PHYSIOLOGY  Zinc
       Fingers  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).

