ArticleProceedings of the National Academy of Sciences of the United States of America2001
DNA binding induces dissociation of the multimeric form of HIV-1 integrase: a time-resolved fluorescence anisotropy study.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Structural Impact of Ex Vivo Resistance Mutations on HIV-1 Integrase Polymers Induced by Allosteric Inhibitors.Journal of molecular biology · 2025Article
- Structure of a HIV-1 IN-Allosteric inhibitor complex at 2.93 Å resolution: Routes to inhibitor optimization.PLoS pathogens · 2023Article
- Review
- Allosteric HIV Integrase Inhibitors Promote Formation of Inactive Branched Polymers via Homomeric Carboxy-Terminal Domain Interactions.Structure (London, England : 1993) · 2021Article
- Fluorescence Quenching of Two Coumarin-3-carboxylic Acids by Trivalent Lanthanide Ions.Journal of fluorescence · 2017Article
- Rotational and vibrational dynamics in the excited electronic state of deprotonated and protonated fluorescein studied by time-resolved photofragmentation in an ion trap.Structural dynamics (Melville, N.Y.) · 2016Article
- Different Pathways Leading to Integrase Inhibitors Resistance.Frontiers in microbiology · 2016Review
- Allosteric modulation of protein oligomerization: an emerging approach to drug design.Frontiers in chemistry · 2014Review
- DEAD-box RNA helicase domains exhibit a continuum between complete functional independence and high thermodynamic coupling in nucleotide and RNA duplex recognition.Nucleic acids research · 2014Article
- Article
- Solution conformations of prototype foamy virus integrase and its stable synaptic complex with U5 viral DNA.Structure (London, England : 1993) · 2012Article
- Dynamic dissociating homo-oligomers and the control of protein function.Archives of biochemistry and biophysics · 2012Review
- Article
- Characterization of photophysical and base-mimicking properties of a novel fluorescent adenine analogue in DNA.Nucleic acids research · 2011Article
- Mass spectrometric characterization of oligomers in Pseudomonas aeruginosa azurin solutions.The journal of physical chemistry. B · 2011Article
- Synthesis, electrochemical, and optical properties of new fluorescent, substituted thieno[3,2-b][1]benzothiophenes.Journal of fluorescence · 2010Article
- Structural properties of HIV integrase. Lens epithelium-derived growth factor oligomers.The Journal of biological chemistry · 2010Article
- 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
- Oligonucleotide-based assays for integrase activity.Methods (San Diego, Calif.) · 2009Review
- Mechanistic and pharmacological analyses of HIV-1 integration.Methods (San Diego, Calif.) · 2009Article
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Authors and funding
7 authors.
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Abstract
Self-assembly of HIV-1 integrase (IN) in solution has been studied previously by time-resolved fluorescence, using tryptophan anisotropy decay. This approach provides information on the size of macromolecules via the determination of rotational correlation times (theta). We have shown that, at submicromolar concentration, IN is characterized by a long rotational correlation time (theta(20 degrees C) = 90-100 ns) corresponding to a high-order oligomeric form, likely a tetramer. In the present work, we investigated the self-assembly properties of the DNA-bound IN by using three independent fluorophores. Under enzymatic assay conditions (10(-7) M IN, 2 x 10(-8) M DNA), using either fluorescein-labeled or fluorescent guanosine analog-containing oligonucleotides that mimic a viral end long terminal repeat sequence, we found that the DNA-IN complex was characterized by shorter theta(20 degrees C) values of 15.5-19.5 and 23-27 ns, calculated from experiments performed at 25 degrees C and 37 degrees C, respectively. These results were confirmed by monitoring the Trp anisotropy decay as a function of the DNA substrate concentration: the theta of IN shifted from 90-100 ns to lower values (<30 ns) upon increasing the DNA concentration. Again, the normalized theta(20 degrees C) values were significantly higher when monitored at 37 degrees C as compared with 25 degrees C. These results indicate that upon binding the viral DNA end, the multimeric enzyme undergoes a dissociation, most likely into a homogeneous monomeric form at 25 degrees C and into a monomer-dimer equilibrium at 37 degrees C.
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