ArticleBiochemistry2009
Kinetics of association and dissociation of HIV-1 reverse transcriptase subunits.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 25 citations in OpenAlex.
- Targeting the Structural Maturation Pathway of HIV-1 Reverse Transcriptase.Biomolecules · 2023Article
- Conformational Changes in HIV-1 Reverse Transcriptase that Facilitate Its Maturation.Structure (London, England : 1993) · 2019Article
- HIV-1 Reverse Transcriptase: A Metamorphic Protein with Three Stable States.Structure (London, England : 1993) · 2019Review
- Effect of tRNA on the Maturation of HIV-1 Reverse Transcriptase.Journal of molecular biology · 2018Article
- The HIV-1 p66 homodimeric RT exhibits different conformations in the binding-competent and -incompetent NNRTI site.Proteins · 2017Article
- FRET analysis of HIV-1 Gag and GagPol interactions.FEBS open bio · 2017Article
- Identification of drivers for the metamorphic transition of HIV-1 reverse transcriptase.The Biochemical journal · 2017Article
- Structural Maturation of HIV-1 Reverse Transcriptase-A Metamorphic Solution to Genomic Instability.Viruses · 2016Review
- Unfolding the HIV-1 reverse transcriptase RNase H domain--how to lose a molecular tug-of-war.Nucleic acids research · 2016Article
- Article
- Distance mapping in proteins using fluorescence spectroscopy: tyrosine, like tryptophan, quenches bimane fluorescence in a distance-dependent manner.Biochemistry · 2014Article
- The p66 immature precursor of HIV-1 reverse transcriptase.Proteins · 2014Article
- Selective unfolding of one Ribonuclease H domain of HIV reverse transcriptase is linked to homodimer formation.Nucleic acids research · 2014Article
- Slow, reversible, coupled folding and binding of the spectrin tetramerization domain.Biophysical journal · 2012Article
- Biotinylation, a post-translational modification controlled by the rate of protein-protein association.The Journal of biological chemistry · 2011Article
- Efavirenz binding site in HIV-1 reverse transcriptase monomers.Biochemistry · 2010Article
- Distance mapping in proteins using fluorescence spectroscopy: the tryptophan-induced quenching (TrIQ) method.Biochemistry · 2010Article
- The association−dissociation behavior of the ApoE proteins: kinetic and equilibrium studies.Biochemistry · 2010Article
- Homodimerization of the p51 subunit of HIV-1 reverse transcriptase.Biochemistry · 2010Article
- Efavirenz binding to HIV-1 reverse transcriptase monomers and dimers.Biochemistry · 2010Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The biologically active form of HIV-1 reverse transcriptase (RT) is the p66/p51 heterodimer. The process of maturation of the heterodimer from precursor proteins is poorly understood. Previous studies indicated that association of p66 and p51 is very slow. Three techniques, a pre-steady-state activity assay, intrinsic tryptophan fluorescence, and a FRET assay, were used to monitor the dimerization kinetics of RT. Kinetic experiments were conducted with purified p66 and p51 proteins in aqueous buffer. All three techniques gave essentially the same results. The dissociation kinetics of p66/p51 were first-order with rate constants (k(diss)) of approximately 4 x 10(-6) s(-1) (t(1/2) = 48 h). The association kinetics of p66 and p51 were concentration-dependent with second-order rate constants (k(ass)) of approximately 1.7 M(-1) s(-1) for the simple bimolecular association reaction. The implications of slow dimerization of p66/p51 for the maturation process are discussed. A reaction-controlled model invoking conformational selection is proposed to explain the slow protein-protein association kinetics.
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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.