ArticleProtein science : a publication of the Protein Society2011
Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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40 citing papers in PubMed, 71 citations in OpenAlex.
- Toward unraveling molecular grammars for dsRNA-binding proteins: substrate recognition to binding mechanisms.BMB reports · 2025Review
- HPD is an RNA-Binding Protein Sustaining Ovarian Cancer Cell Glycolysis, Tumor Growth, and Drug Resistance.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Dimerization of ADAR1 modulates site-specificity of RNA editing.Nature communications · 2024Article
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- Mutations in the WG and GW motifs of the three RNA silencing suppressors of grapevine fanleaf virus alter their systemic suppression ability and affect virus infectivity.Frontiers in microbiology · 2024Article
- Inherent conformational plasticity in dsRBDs enables interaction with topologically distinct RNAs.Biophysical journal · 2022Article
- Opposite actions of two dsRNA-binding proteins PACT and TRBP on RIG-I mediated signaling.The Biochemical journal · 2021Article
- A Glimpse of "Dicer Biology" Through the Structural and Functional Perspective.Frontiers in molecular biosciences · 2021Review
- Structural basis of siRNA recognition by TRBP double-stranded RNA binding domains.The EMBO journal · 2018Article
- Conserved asymmetry underpins homodimerization of Dicer-associated double-stranded RNA-binding proteins.Nucleic acids research · 2017Article
- Molecular basis for asymmetry sensing of siRNAs by the Drosophila Loqs-PD/Dcr-2 complex in RNA interference.Nucleic acids research · 2017Article
- RNA Scanning of a Molecular Machine with a Built-in Ruler.Journal of the American Chemical Society · 2017Article
- TRBP ensures efficient Dicer processing of precursor microRNA in RNA-crowded environments.Nature communications · 2016Article
- Visualizing repetitive diffusion activity of double-strand RNA binding proteins by single molecule fluorescence assays.Methods (San Diego, Calif.) · 2016Review
- Binding by TRBP-dsRBD2 Does Not Induce Bending of Double-Stranded RNA.Biophysical journal · 2016Article
- Recombinant hTRBP and hPACT Modulate hAgo2-Catalyzed siRNA-Mediated Target RNA Cleavage In Vitro.PloS one · 2016Article
- Dynamic profiling of double-stranded RNA binding proteins.Nucleic acids research · 2015Article
- Induced folding in RNA recognition by Arabidopsis thaliana DCL1.Nucleic acids research · 2015Article
- Dicer-TRBP complex formation ensures accurate mammalian microRNA biogenesis.Molecular cell · 2015Article
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The TAR RNA-binding Protein (TRBP) is a double-stranded RNA (dsRNA)-binding protein, which binds to Dicer and is required for the RNA interference pathway. TRBP consists of three dsRNA-binding domains (dsRBDs). The first and second dsRBDs (dsRBD1 and dsRBD2, respectively) have affinities for dsRNA, whereas the third dsRBD (dsRBD3) binds to Dicer. In this study, we prepared the single domain fragments of human TRBP corresponding to dsRBD1 and dsRBD2 and solved the crystal structure of dsRBD1 and the solution structure of dsRBD2. The two structures contain an α-β-β-β-α fold, which is common to the dsRBDs. The overall structures of dsRBD1 and dsRBD2 are similar to each other, except for a slight shift of the first α helix. The residues involved in dsRNA binding are conserved. We examined the small interfering RNA (siRNA)-binding properties of these dsRBDs by isothermal titration colorimetry measurements. The dsRBD1 and dsRBD2 fragments both bound to siRNA, with dissociation constants of 220 and 113 nM, respectively. In contrast, the full-length TRBP and its fragment with dsRBD1 and dsRBD2 exhibited much smaller dissociation constants (0.24 and 0.25 nM, respectively), indicating that the tandem dsRBDs bind simultaneously to one siRNA molecule. On the other hand, the loop between the first α helix and the first β strand of dsRBD2, but not dsRBD1, has a Trp residue, which forms hydrophobic and cation-π interactions with the surrounding residues. A circular dichroism analysis revealed that the thermal stability of dsRBD2 is higher than that of dsRBD1 and depends on the Trp residue.
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