ArticleJournal of molecular biology2011
Single-molecule studies reveal that DEAD box protein DDX1 promotes oligomerization of HIV-1 Rev on the Rev response element.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.
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Who cites it
37 citing papers in PubMed, 1 synthesis or guideline pooled it.
- HIV Genome-Wide Protein Associations: a Review of 30 Years of Research.Microbiology and molecular biology reviews : MMBR · 2016Pooled it
- Enzymology of the metazoan tRNA ligase complex: a lifetime in cycles.Cellular and molecular life sciences : CMLS · 2026Review
- DDX1 methylation mediated MATR3 splicing regulates intervertebral disc degeneration by initiating chromatin reprogramming.Nature communications · 2025Article
- Viral Subversion of the Chromosome Region Maintenance 1 Export Pathway and Its Consequences for the Cell Host.Viruses · 2023Review
- Review
- Binding stoichiometry and structural model of the HIV-1 Rev/importin β complex.Life science alliance · 2022Article
- DEAD-ly Affairs: The Roles of DEAD-Box Proteins on HIV-1 Viral RNA Metabolism.Frontiers in cell and developmental biology · 2022Review
- HIV Rev-isited.Open biology · 2020Review
- Review
- Highly Mutable Linker Regions Regulate HIV-1 Rev Function and Stability.Scientific reports · 2019Article
- Single-molecule fluorescence imaging: Generating insights into molecular interactions in virology.Journal of biosciences · 2018Review
- Differential Effects of Strategies to Improve the Transduction Efficiency of Lentiviral Vector that Conveys an Anti-HIV Protein, Nullbasic, in Human T Cells.Virologica Sinica · 2018Article
- A Survey of DDX21 Activity During Rev/RRE Complex Formation.Journal of molecular biology · 2018Article
- A DEAD-box protein acts through RNA to promote HIV-1 Rev-RRE assembly.Nucleic acids research · 2017Article
- A DEAD-Box Helicase Mediates an RNA Structural Transition in the HIV-1 Rev Response Element.Journal of molecular biology · 2017Article
- Oligomeric viral proteins: small in size, large in presence.Critical reviews in biochemistry and molecular biology · 2016Review
- A structurally plastic ribonucleoprotein complex mediates post-transcriptional gene regulation in HIV-1.Wiley interdisciplinary reviews. RNA · 2016Review
- HIV-1 Nef-associated Factor 1 Enhances Viral Production by Interacting with CRM1 to Promote Nuclear Export of Unspliced HIV-1 gag mRNA.The Journal of biological chemistry · 2016Article
- Loss of the Drosophila melanogaster DEAD box protein Ddx1 leads to reduced size and aberrant gametogenesis.Developmental biology · 2015Article
- Structure of the SPRY domain of the human RNA helicase DDX1, a putative interaction platform within a DEAD-box protein.Acta crystallographica. Section F, Structural biology communications · 2015Article
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6 authors.
Funding
Abstract
Oligomeric assembly of Rev on the Rev response element (RRE) is essential for the nuclear export of unspliced and singly spliced human immunodeficiency virus type 1 viral mRNA transcripts. Several host factors, including the human DEAD box protein DDX1, are also known to be required for efficient Rev function. In this study, spontaneous assembly and dissociation of individual Rev-RRE complexes in the presence or absence of DDX1 were observed in real time via single-molecule total internal reflection fluorescence microscopy. Binding of up to eight fluorescently labeled Rev monomers to a single RRE molecule was visualized, and the event frequencies and corresponding binding and dissociation rates for the different Rev-RRE stoichiometries were determined. The presence of DDX1 eliminated a second kinetic phase present during the initial Rev binding step, attributed to nonproductive nucleation events, resulting in increased occurrence of higher-order Rev-RRE stoichiometries. This effect was further enhanced upon the addition of a non-hydrolyzable ATP analog (adenylyl-imidophosphate), whereas ADP had no effect beyond that of DDX1 alone. Notably, the first three Rev monomer binding events were accelerated in the presence of DDX1 and adenylyl-imidophosphate, while the dissociation rates remained unchanged. Measurements performed across a range of DDX1 concentrations suggest that DDX1 targets Rev rather than the RRE to promote oligomeric assembly. Moreover, DDX1 is able to restore the oligomerization activity of a Rev mutant that is otherwise unable to assemble on the RRE beyond a monomeric complex. Taken together, these results suggest that DDX1 acts as a cellular cofactor by promoting oligomerization of Rev on the RRE.
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