ArticleNucleic acids research2004
Biochemical and random mutagenesis analysis of the region carrying the catalytic E152 amino acid of HIV-1 integrase.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Quantitative analysis of the time-course of viral DNA forms during the HIV-1 life cycle.Retrovirology · 2013Article
- Soluble expression, purification and characterization of the full length IS2 Transposase.Mobile DNA · 2011Article
- Selection of bacteriophage lambda integrases with altered recombination specificity by in vitro compartmentalization.Nucleic acids research · 2010Article
- Contribution of the C-terminal region within the catalytic core domain of HIV-1 integrase to yeast lethality, chromatin binding and viral replication.Retrovirology · 2008Article
- Small-angle X-ray characterization of the nucleoprotein complexes resulting from DNA-induced oligomerization of HIV-1 integrase.Nucleic acids research · 2007Article
- Dihydroxythiophenes are novel potent inhibitors of human immunodeficiency virus integrase with a diketo acid-like pharmacophore.Journal of virology · 2006Article
- Chromosomal integration of LTR-flanked DNA in yeast expressing HIV-1 integrase: down regulation by RAD51.Nucleic acids research · 2006Article
- A substitution in rous sarcoma virus integrase that separates its two biologically relevant enzymatic activities.Journal of virology · 2005Article
- HIV-1 integrase crosslinked oligomers are active in vitro.Nucleic acids research · 2005Article
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Authors and funding
8 authors.
Funding
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Abstract
HIV-1 integrase (IN) catalyzes the integration of the proviral DNA into the cellular genome. The catalytic triad D64, D116 and E152 of HIV-1 IN is involved in the reaction mechanism and the DNA binding. Since the integration and substrate binding processes are not yet exactly known, we studied the role of amino acids localized in the catalytic site. We focused our interest on the V151E152S153 region. We generated random mutations inside this domain and selected mutated active INs by using the IN-induced yeast lethality assay. In vitro analysis of the selected enzymes showed that the IN nuclease activities (specific 3'-processing and non-sequence-specific endonuclease), the integration and disintegration reactions and the binding of the various DNA substrates were affected differently. Our results support the hypothesis that the three reactions may involve different DNA binding sites, enzyme conformations or mechanisms. We also show that the V151E152S153 region involvement in the integration reaction is more important than for the 3'-processing activity and can be involved in the recognition of DNA. The IN mutants may lead to the development of new tools for studying the integration reaction, and could serve as the basis for the discovery of integration-specific inhibitors.
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