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M9640544.TXT
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1996-03-04
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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).