Document 0409
 DOCN  M9490409
 TI    The core and carboxyl-terminal domains of the integrase protein of human
       immunodeficiency virus type 1 each contribute to nonspecific DNA
       binding.
 DT    9411
 AU    Engelman A; Hickman AB; Craigie R; Laboratory of Molecular Biology,
       National Institute of Diabetes; and Digestive and Kidney Diseases,
       National Institutes of Health,; Bethesda, MD 20892.
 SO    J Virol. 1994 Sep;68(9):5911-7. Unique Identifier : AIDSLINE
       MED/94335108
 AB    The integrase protein of human immunodeficiency virus type 1 removes two
       nucleotides from the 3' ends of reverse-transcribed human
       immunodeficiency virus type 1 DNA (3' processing) and covalently inserts
       the processed ends into a target DNA (DNA strand transfer). Mutant
       integrase proteins that lack the amino-and/or carboxyl-terminal domains
       are incapable of catalyzing 3' processing and DNA strand transfer but
       are competent for an apparent reversal of the DNA strand transfer
       reaction (disintegration) in vitro. Here, we investigate the binding of
       integrase to DNA by UV cross-linking. Cross-linked complexes form with a
       variety of DNA substrates independent of the presence of divalent metal
       ion. Analysis with amino- and carboxyl-terminal deletion mutant proteins
       shows that residues 213 to 266 of the 288-residue protein are required
       for efficient cross-linking in the absence of divalent metal ion.
       Carboxyl-terminal deletion mutants that lack this region efficiently
       cross-link only to the branched disintegration DNA substrate, and this
       reaction is dependent on the presence of metal ion. Both the core and
       C-terminal domains of integrase therefore contribute to nonspecific DNA
       binding.
 DE    DNA Nucleotidyltransferases/*METABOLISM  DNA-Binding
       Proteins/*METABOLISM  DNA, Single-Stranded/METABOLISM  DNA,
       Viral/METABOLISM  HIV-1/*ENZYMOLOGY  Photochemistry  Recombinant
       Proteins  Sequence Deletion  Structure-Activity Relationship  Support,
       U.S. Gov't, P.H.S.  Ultraviolet Rays  *Virus Integration  JOURNAL
       ARTICLE

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