Characterization of the DNA-binding activity of HIV-1 integrase using a filter binding assay. NLM AIDSLINE Important note: Information in this article was accurate in 1996. The state of the art may have changed since the publication date.

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Characterization of the DNA-binding activity of HIV-1 integrase using a filter binding assay.

Biochem Biophys Res Commun. 1995 Dec 26;217(3):802-10. Unique Identifier : AIDSLINE MED/96125314
Haugan IR; Nilsen BM; Worland S; Olsen L; Helland DE; Laboratory of Biotechnology, University of Bergen, Norway.

Abstract: 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.
Keywords: 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 ARTICLEKWDbasesequencedna-bindingproteins/KWDmetabolismendodeoxyribonucleases/KWDmetabolismhiv-1/KWDenzymologymacromolecularsystemsmolecularsequencedataoligodeoxyribonucleotides/chemistrysupport,uKWDsKWDgov't,pKWDhKWDs
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M9640036

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