title: Efficient magnesium-dependent human immunodeficiency virus type 1 integrase activity.
abstract: The integrase protein from human immunodeficiency virus type 1 (HIV-1) has generally been reported to require Mn2+ for efficient in vitro activity. We have reexamined the divalent metal ion requirements of HIV-1 integrase and find that the protein is capable of promoting efficient 3' processing and DNA strand transfer with either Mn2+ or Mg2+. The metal ion preference depended upon the reaction conditions. HIV-1 integrase displayed significantly less nonspecific nuclease activity in reaction mixtures containing Mg2+ than it did under the previously described reaction conditions with mixtures containing Mn2+.
authors.affiliation: Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892-0560, USA.
authors.forename: A
authors.initials: A
authors.lastname: Engelman
authors.forename: R
authors.initials: R
authors.lastname: Craigie
mesh_terms: D001483:Base Sequence; D004254:DNA Nucleotidyltransferases / Q000378:metabolism*; D004279:DNA, Viral / Q000737:chemistry / Q000378:metabolism; D015497:HIV-1 / Q000201:enzymology*; D019426:Integrases; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology*; D008345:Manganese / Q000494:pharmacology*; D008957:Models, Genetic; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides / Q000378:metabolism; D013379:Substrate Specificity; D016662:Virus Integration
chemical_list: D004279:DNA, Viral; D009838:Oligodeoxyribonucleotides; D008345:Manganese; D004254:DNA Nucleotidyltransferases; D019426:Integrases; D008274:Magnesium