ArticleBiophysical journal2013
The arginine-rich RNA-binding motif of HIV-1 Rev is intrinsically disordered and folds upon RRE binding.
Article in Biophysical journal, 2013. 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.
- Protein Nanocages as Versatile Vectors for Nucleic Acid Delivery: Main Systems and Their Loading Mechanisms.Molecular biotechnology · 2026Review
- Characterization of nucleolar localization signals in the avian infectious bronchitis virus nucleocapsid protein and their critical role in viral replication.Journal of virology · 2026Article
- Single-stranded nucleic acid binding enhances the in vitro catalytic activity of Chikungunya virus nsP2 protease.BBA advances · 2026Article
- Accurate Generation of Conformational Ensembles for Intrinsically Disordered Proteins with IDPFold.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Structural integrity and side-chain interaction at the loop region of the bridge helix modulate Cas9 substrate discrimination.Nucleic acids research · 2025Article
- Ghost authors revealed: The structure and function of human NWiley interdisciplinary reviews. RNA · 2023Review
- Vital for Viruses: Intrinsically Disordered Proteins.Journal of molecular biology · 2023Review
- Binding stoichiometry and structural model of the HIV-1 Rev/importin β complex.Life science alliance · 2022Article
- Tuning Rex rules HTLV-1 pathogenesis.Frontiers in immunology · 2022Review
- Role of salt-bridging interactions in recognition of viral RNA by arginine-rich peptides.Biophysical journal · 2021Article
- Article
- The bridge helix of Cas12a imparts selectivity in cis-DNA cleavage and regulates trans-DNA cleavage.FEBS letters · 2021Article
- Review
- Environment-Specific Force Field for Intrinsically Disordered and Ordered Proteins.Journal of chemical information and modeling · 2020Article
- Intrinsically disordered proteins of viruses: Involvement in the mechanism of cell regulation and pathogenesis.Progress in molecular biology and translational science · 2020Review
- The Capsid Protein of Hepatitis E Virus Inhibits Interferon Induction via Its N-terminal Arginine-Rich Motif.Viruses · 2019Article
- RNA-protein interactions: disorder, moonlighting and junk contribute to eukaryotic complexity.Open biology · 2019Review
- Bridge Helix of Cas9 Modulates Target DNA Cleavage and Mismatch Tolerance.Biochemistry · 2019Article
- Computational Studies of Intrinsically Disordered Proteins.The journal of physical chemistry. B · 2018Article
- A new HIV-1 Rev structure optimizes interaction with target RNA (RRE) for nuclear export.Journal of structural biology · 2018Article
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3 authors.
Funding
Abstract
Arginine-rich motifs (ARMs) capable of binding diverse RNA structures play critical roles in transcription, translation, RNA trafficking, and RNA packaging. The regulatory HIV-1 protein Rev is essential for viral replication and belongs to the ARM family of RNA-binding proteins. During the early stages of the HIV-1 life cycle, incompletely spliced and full-length viral mRNAs are very inefficiently recognized by the splicing machinery of the host cell and are subject to degradation in the cell nucleus. These transcripts harbor the Rev Response Element (RRE), which orchestrates the interaction with the Rev ARM and the successive Rev-dependent mRNA export pathway. Based on established criteria for predicting intrinsic disorder, such as hydropathy, combined with significant net charge, the very basic primary sequences of ARMs are expected to adopt coil-like structures. Thus, we initiated this study to investigate the conformational changes of the Rev ARM associated with RNA binding. We used multidimensional NMR and circular dichroism spectroscopy to monitor the observed structural transitions, and described the conformational landscapes using statistical ensemble and molecular-dynamics simulations. The combined spectroscopic and simulated results imply that the Rev ARM is intrinsically disordered not only as an isolated peptide but also when it is embedded into an oligomerization-deficient Rev mutant. RRE recognition triggers a crucial coil-to-helix transition employing an induced-fit mechanism.
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