Efficient magnesium-dependent human immunodeficiency virus type 1 integrase activity.
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+.
Engelman
A
A
Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892-0560, USA.
Craigie
R
R
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
D004279:DNA, Viral; D009838:Oligodeoxyribonucleotides; D008345:Manganese; D004254:DNA Nucleotidyltransferases; D019426:Integrases; D008274:Magnesium