ArticleBiopolymers2023
Biochemical and biophysical characterization of the nucleic acid binding properties of the RNA/DNA binding protein EWS.
Article in Biopolymers, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- FUS and TAF15 safeguard the critical functions of the ribonucleoprotein network formed by EWSR1 and newly synthesized RNA.bioRxiv : the preprint server for biology · 2026Article
- Molecular basis of EWS interdomain self-association and its role in condensate formation.Protein science : a publication of the Protein Society · 2025Article
- The Spliceosomal Peptidyl Prolyl Isomerase Like 1 Interacts with the Low-Complexity Domain of the RNA Binding Protein EWS Modulating Its Phase Separation Behavior.Biochemistry · 2025Article
- Purification of Low-Complexity Domain Proteins FUS, EWSR1, and Their Fusions.Current protocols · 2025Article
- Small molecules reveal differential shifts in stability and protein binding for G-quadruplex RNA.bioRxiv : the preprint server for biology · 2025Article
- Review
- Ewing Sarcoma Related protein 1 recognizes R-loops by binding DNA forks.Biopolymers · 2024Article
- Ewing Sarcoma Related protein 1 recognizes R-loops by binding DNA forks.bioRxiv : the preprint server for biology · 2024Article
- Endogenous EWSR1 Exists in Two Visual Modalities That Reflect Its Associations with Nucleic Acids and Concentration at Sites of Active Transcription.Molecular and cellular biology · 2024Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
EWS is a member of the FET family of RNA/DNA binding proteins that regulate crucial phases of nucleic acid metabolism. EWS comprises an N-terminal low-complexity domain (LCD) and a C-terminal RNA-binding domain (RBD). The RBD is further divided into three RG-rich regions, which flank an RNA-recognition motif (RRM) and a zinc finger (ZnF) domain. Recently, EWS was shown to regulate R-loops in Ewing sarcoma, a pediatric bone and soft-tissue cancer in which a chromosomal translocation fuses the N-terminal LCD of EWS to the C-terminal DNA binding domain of the transcription factor FLI1. Though EWS was shown to directly bind R-loops, the binding mechanism was not elucidated. In the current study, the RBD of EWS was divided into several constructs, which were subsequently assayed for binding to various nucleic acid structures expected to form at R-loops, including RNA stem-loops, DNA G-quadruplexes, and RNA:DNA hybrids. EWS interacted with all three nucleic acid structures with varying affinities and multiple domains contributed to binding each substrate. The RRM and RG2 region appear to bind nucleic acids promiscuously while the ZnF displayed more selectivity for single-stranded structures. With these results, the structural underpinnings of EWS recognition and binding of R-loops and other nucleic acid structures is better understood.
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