Document 0210
 DOCN  M9440210
 TI    Activities of the feline immunodeficiency virus integrase protein
       produced in Escherichia coli.
 DT    9404
 AU    Vink C; van der Linden KH; Plasterk RH; Division of Molecular Biology,
       The Netherlands Cancer Institute,; Amsterdam.
 SO    J Virol. 1994 Mar;68(3):1468-74. Unique Identifier : AIDSLINE
       MED/94149835
 AB    Retroviral DNA integration requires the activity of at least one viral
       protein, the integrase (IN) protein. We cloned and expressed the
       integrase gene of feline immunodeficiency virus (FIV) in Escherichia
       coli as a fusion to the malE gene and purified the IN fusion protein by
       affinity chromatography. The protein is active in site-specific cleavage
       of the viral DNA ends, DNA strand transfer, and disintegration. FIV IN
       has a relaxed viral DNA substrate requirement: it cleaves and integrates
       FIV DNA termini, human immunodeficiency virus DNA ends, and Moloney
       murine leukemia virus DNA ends with high efficiencies. In the cleavage
       reaction, IN exposes a specific phosphodiester bond near the viral DNA
       end to nucleophilic attack. In vitro, either H2O, glycerol, or the 3' OH
       group of the viral DNA terminus can serve as nucleophile in this
       reaction. We found that FIV IN preferentially uses the 3' OH ends of the
       viral DNA as nucleophile, whereas HIV IN protein preferentially uses H2O
       and glycerol as nucleophiles.
 DE    Amino Acid Sequence  Base Sequence  Cloning, Molecular  Comparative
       Study  DNA Insertion Elements  DNA
       Nucleotidyltransferases/GENETICS/ISOLATION & PURIF/  *METABOLISM
       DNA-Binding Proteins/METABOLISM  Escherichia coli/GENETICS
       Immunodeficiency Virus, Feline/*ENZYMOLOGY  Molecular Sequence Data
       Recombinant Fusion Proteins/ISOLATION & PURIF/METABOLISM  Sequence
       Homology, Amino Acid  Substrate Specificity  Support, Non-U.S. Gov't
       Virus Integration/PHYSIOLOGY  JOURNAL ARTICLE

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