ArticleProceedings of the National Academy of Sciences of the United States of America2002
Identification of specific HIV-1 reverse transcriptase contacts to the viral RNA:tRNA complex by mass spectrometry and a primary amine selective reagent.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 58 citations in OpenAlex.
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- Protein modification by adenine propenal.Chemical research in toxicology · 2014Article
- Mass spectrometry tools for analysis of intermolecular interactions.Methods in molecular biology (Clifton, N.J.) · 2012Article
- Broad-spectrum aptamer inhibitors of HIV reverse transcriptase closely mimic natural substrates.Nucleic acids research · 2011Article
- Protein footprinting in a complex milieu: identifying the interaction surfaces of the chemotaxis adaptor protein CheW.Journal of molecular biology · 2011Article
- Cross-talk between the catalytic core and the regulatory domain in cystathionine β-synthase: study by differential covalent labeling and computational modeling.Biochemistry · 2010Article
- Elucidating the higher-order structure of biopolymers by structural probing and mass spectrometry: MS3D.Journal of mass spectrometry : JMS · 2010Article
- Reverse Transcriptase and Cellular Factors: Regulators of HIV-1 Reverse Transcription.Viruses · 2009Article
- Probing conformational changes of human DNA polymerase lambda using mass spectrometry-based protein footprinting.Journal of molecular biology · 2009Article
- A quantitative strategy to detect changes in accessibility of protein regions to chemical modification on heterodimerization.Protein science : a publication of the Protein Society · 2009Article
- Mass spectrometry-based footprinting of protein-protein interactions.Methods (San Diego, Calif.) · 2009Article
- Mechanistic and pharmacological analyses of HIV-1 integration.Methods (San Diego, Calif.) · 2009Article
- Development and evaluation of a structural model for SF1B helicase Dda.Biochemistry · 2009Article
- Novel bimodular DNA aptamers with guanosine quadruplexes inhibit phylogenetically diverse HIV-1 reverse transcriptases.Nucleic acids research · 2008Article
- Dynamic modulation of HIV-1 integrase structure and function by cellular lens epithelium-derived growth factor (LEDGF) protein.The Journal of biological chemistry · 2008Article
- Vinylogous ureas as a novel class of inhibitors of reverse transcriptase-associated ribonuclease H activity.ACS chemical biology · 2008Article
- DNA-dependent conformational changes in the Ku heterodimer.Biochemistry · 2008Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have devised a high-resolution protein footprinting methodology to dissect HIV-1 reverse transcriptase (RT) contacts to the viral RNA:tRNA complex. The experimental strategy included modification of surface-exposed lysines in RT and RT-viral RNA:tRNA complexes by the primary amine selective reagent NHS-biotin, SDSPAGE separation of p66 and p51 polypeptides, in gel proteolysis, and comparative mass spectrometric analysis of peptide fragments. The lysines modified in free RT but protected from biotinylation in the nucleoprotein complex were readily revealed by this approach. Results of a control experiment examining the RT-DNA:DNA complex were in excellent agreement with the crystal structure data on the identical complex. Probing the RT-viral RNA:tRNA complex revealed that a majority of protein contacts are located in the primer-template binding cleft in common with the RT-DNA:DNA and RT-RNA:DNA species. However, our footprinting data indicate that the p66 fingers subdomain makes additional contacts to the viral RNA:tRNA specific for this complex and not detected with DNA:DNA. The protein footprinting method described herein has a generic application for high-resolution solution structural studies of multiprotein-nucleic acid contacts.
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