ArticleNucleic acids research2008
In vitro initial attachment of HIV-1 integrase to viral ends: control of the DNA specific interaction by the oligomerization state.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 31 citations in OpenAlex.
- Carboxylate-functionalized foldamer inhibitors of HIV-1 integrase and Topoisomerase 1: artificial analogues of DNA mimic proteins.Nucleic acids research · 2019Article
- Two-long terminal repeat (LTR) DNA circles are a substrate for HIV-1 integrase.The Journal of biological chemistry · 2019Article
- Single helically folded aromatic oligoamides that mimic the charge surface of double-stranded B-DNA.Nature chemistry · 2018Article
- Modulation of the functional association between the HIV-1 intasome and the nucleosome by histone amino-terminal tails.Retrovirology · 2017Article
- Modulation of chromatin structure by the FACT histone chaperone complex regulates HIV-1 integration.Retrovirology · 2017Article
- The Preserved HTH-Docking Cleft of HIV-1 Integrase Is Functionally Critical.Structure (London, England : 1993) · 2016Article
- Different Pathways Leading to Integrase Inhibitors Resistance.Frontiers in microbiology · 2016Review
- Dual and Opposite Effects of hRAD51 Chemical Modulation on HIV-1 Integration.Chemistry & biology · 2015Article
- Intasome architecture and chromatin density modulate retroviral integration into nucleosome.Retrovirology · 2015Article
- Dual inhibition of HIV-1 replication by integrase-LEDGF allosteric inhibitors is predominant at the post-integration stage.Retrovirology · 2013Article
- A protein ballet around the viral genome orchestrated by HIV-1 reverse transcriptase leads to an architectural switch: from nucleocapsid-condensed RNA to Vpr-bridged DNA.Virus research · 2013Article
- Structural and functional role of INI1 and LEDGF in the HIV-1 preintegration complex.PloS one · 2013Article
- Article
- Stimulation of the human RAD51 nucleofilament restricts HIV-1 integration in vitro and in infected cells.Journal of virology · 2012Article
- Mutations affecting interaction of integrase with TNPO3 do not prevent HIV-1 cDNA nuclear import.Retrovirology · 2011Article
- The HIV-1 integrase monomer induces a specific interaction with LTR DNA for concerted integration.Biochemistry · 2011Article
- Structure-analysis of the HIV-1 integrase Y143C/R raltegravir resistance mutation in association with the secondary mutation T97A.Antimicrobial agents and chemotherapy · 2011Article
- Functional coupling between HIV-1 integrase and the SWI/SNF chromatin remodeling complex for efficient in vitro integration into stable nucleosomes.PLoS pathogens · 2011Article
- The HIV-1 integrase α4-helix involved in LTR-DNA recognition is also a highly antigenic peptide element.PloS one · 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
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Authors and funding
7 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
HIV-1 integrase (IN) oligomerization and DNA recognition are crucial steps for the subsequent events of the integration reaction. Recent advances described the involvement of stable intermediary complexes including dimers and tetramers in the in vitro integration processes, but the initial attachment events and IN positioning on viral ends are not clearly understood. In order to determine the role of the different IN oligomeric complexes in these early steps, we performed in vitro functional analysis comparing IN preparations having different oligomerization properties. We demonstrate that in vitro IN concerted integration activity on a long DNA substrate containing both specific viral and nonspecific DNA sequences is highly dependent on binding of preformed dimers to viral ends. In addition, we show that IN monomers bound to nonspecific DNA can also fold into functionally different oligomeric complexes displaying nonspecific double-strand DNA break activity in contrast to the well known single strand cut catalyzed by associated IN. Our results imply that the efficient formation of the active integration complex highly requires the early correct positioning of monomeric integrase or the direct binding of preformed dimers on the viral ends. Taken together the data indicates that IN oligomerization controls both the enzyme specificity and activity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.