ArticleNucleic acids research2007
Small-angle X-ray characterization of the nucleoprotein complexes resulting from DNA-induced oligomerization of HIV-1 integrase.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Different Pathways Leading to Integrase Inhibitors Resistance.Frontiers in microbiology · 2016Review
- HIV-1 integrase multimerization as a therapeutic target.Current topics in microbiology and immunology · 2015Review
- The HIV-1 integrase monomer induces a specific interaction with LTR DNA for concerted integration.Biochemistry · 2011Article
- Structural properties of HIV integrase. Lens epithelium-derived growth factor oligomers.The Journal of biological chemistry · 2010Article
- A cooperative and specific DNA-binding mode of HIV-1 integrase depends on the nature of the metallic cofactor and involves the zinc-containing N-terminal domain.Nucleic acids research · 2010Article
- HIV-1 Integrase-DNA Recognition Mechanisms.Viruses · 2009Article
- Piecing together the structure of retroviral integrase, an important target in AIDS therapy.The FEBS journal · 2009Review
- Catalytically-active complex of HIV-1 integrase with a viral DNA substrate binds anti-integrase drugs.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- An unusual helix turn helix motif in the catalytic core of HIV-1 integrase binds viral DNA and LEDGF.PloS one · 2009Article
- Integrase and integration: biochemical activities of HIV-1 integrase.Retrovirology · 2008Review
- In vitro initial attachment of HIV-1 integrase to viral ends: control of the DNA specific interaction by the oligomerization state.Nucleic acids research · 2008Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
HIV-1 integrase (IN) catalyses integration of a DNA copy of the viral genome into the host genome. Specific interactions between retroviral IN and long terminal repeats (LTR) are required for this insertion. To characterize quantitatively the influence of the determinants of DNA substrate specificity on the oligomerization status of IN, we used the small-angle X-ray scattering (SAXS) technique. Under certain conditions in the absence of ODNs IN existed only as monomers. IN preincubation with specific ODNs led mainly to formation of dimers, the relative amount of which correlated well with the increase in the enzyme activity in the 3'-processing reaction. Under these conditions, tetramers were scarce. Non-specific ODNs stimulated formation of catalytically inactive dimers and tetramers. Complexes of monomeric, dimeric and tetrameric forms of IN with specific and non-specific ODNs had varying radii of gyration (R(g)), suggesting that the specific sequence-dependent formation of IN tetramers can probably occur by dimerization of two dimers of different structure. From our data we can conclude that the DNA-induced oligomerization of HIV-1 IN is probably of importance to provide substrate specificity and to increase the enzyme activity.
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