ArticleNucleic acids research2018
G-quadruplex binding ability of TLS/FUS depends on the β-spiral structure of the RGG domain.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 62 citations in OpenAlex.
- RNA G-quadruplexes function as a tunable switch of FUS phase separation.Nucleic acids research · 2026Article
- RNA-binding protein transcripts reflect composition of target mRNAs.Nucleic acids research · 2026Article
- Visualizing TERRA RNA G-quadruplex Unfolding in FUS Biomolecular Condensates.Journal of molecular biology · 2026Article
- Photoclick chemistry led to the identification of HELLS as a helicase for DNA G-quadruplexes.Nucleic acids research · 2026Article
- Specificity of the stabilizing interaction between intrinsically disordered protein sequences and G-quadruplexes in RNA.Nucleic acids research · 2026Article
- Transcriptional regulation of telomeric repeat-containing RNA by the G-quadruplex-binding Ewing sarcoma protein.Scientific reports · 2025Article
- RNA G-Quadruplexes Function as a Tunable Switch of FUS Phase Separation.bioRxiv : the preprint server for biology · 2025Article
- Visualizing TERRA RNA G-quadruplex unfolding in FUS biomolecular condensates.bioRxiv : the preprint server for biology · 2025Article
- G-quadruplex structural motifs modulate protein-RNA interactions within the transcriptome.Genome biology · 2025Article
- Visualization of liquid-liquid phase transitions using a tiny G-quadruplex binding protein.Nature communications · 2025Article
- Visualization of liquid-liquid phase transitions using a tiny G-quadruplex binding protein.bioRxiv : the preprint server for biology · 2025Article
- RNA G-quadruplex structure targeting and imaging: recent advances and future directions.RNA (New York, N.Y.) · 2025Review
- The ribonucleoprotein hnRNPA1 mediates binding to RNA and DNA telomeric G-quadruplexes through an RGG-rich region.The Journal of biological chemistry · 2025Article
- The RNA-binding Selectivity of the RGG/RG Motifs of hnRNP U is Abolished by Elements Within the C-terminal Intrinsically Disordered Region.Journal of molecular biology · 2024Article
- Modeling sporadic juvenile ALS in iPSC-derived motor neurons explores the pathogenesis of FUSFrontiers in cellular neuroscience · 2024Article
- Article
- Skipper analysis of eCLIP datasets enables sensitive detection of constrained translation factor binding sites.Cell genomics · 2023Article
- Review
- Biochemical and biophysical characterization of the nucleic acid binding properties of the RNA/DNA binding protein EWS.Biopolymers · 2023Article
- The Fragile X Protein Disordered Regions Bind a Novel RNA Target.Biochemistry · 2022Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RGG domain, defined as closely spaced Arg-Gly-Gly repeats, is a DNA and RNA-binding domain in various nucleic acid-binding proteins. Translocated in liposarcoma (TLS), which is also called FUS, is a protein with three RGG domains, RGG1, RGG2 and RGG3. TLS/FUS binding to G-quadruplex telomere DNA and telomeric repeat-containing RNA depends especially on RGG3, comprising Arg-Gly-Gly repeats with proline- and arginine-rich regions. So far, however, only non-specific DNA and RNA binding of TLS/FUS purified with buffers containing urea and KCl have been reported. Here, we demonstrate that protein purification using a buffer with high concentrations of urea and KCl decreases the G-quadruplex binding abilities of TLS/FUS and RGG3, and disrupts the β-spiral structure of RGG3. Moreover, the Arg-Gly-Gly repeat region in RGG3 by itself cannot form a stable β-spiral structure that binds to the G-quadruplex, because the proline- and arginine-rich regions induce the β-spiral structure and the G-quadruplex-binding ability of RGG3. Our findings suggest that the G-quadruplex-specific binding abilities of TLS/FUS require RGG3 with a β-spiral structure stabilized by adjacent proline- and arginine-regions.
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