ArticleProceedings of the National Academy of Sciences of the United States of America2025
Coding relationship links RNA G-quadruplexes and protein RGG motifs in RNA-binding protein autoregulation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- AND-Logic-Gated Aptamer Switch for Precise Targeting and Regulation of RNA G-Quadruplexes.Angewandte Chemie (International ed. in English) · 2026Article
- RNA G-quadruplexes function as a tunable switch of FUS phase separation.Nucleic acids research · 2026Article
- Bridging technical innovation and computational advances in studies of RNA-protein assemblies.Nature reviews. Genetics · 2026Review
- DNA affects the phenotype of fuel-dependent coacervate droplets.Nature communications · 2026Article
- A deep learning framework for comprehensive prediction of human RNA G-quadruplex-binding proteins.Bioinformatics (Oxford, England) · 2026Article
- RNA G-quadruplexes in oncogene regulation and as emerging targets for cancer therapy.Cell communication and signaling : CCS · 2026Review
- RNA G-quadruplexes promote codon repeat-associated ribosomal frameshifting in human genes.Nucleic acids research · 2026Article
- Nuclear-import receptors remodel the dilute phase to suppress phase transitions of RNA-binding proteins with prion-like domains.bioRxiv : the preprint server for biology · 2025Article
- Article
- RNA G-Quadruplexes Function as a Tunable Switch of FUS Phase Separation.bioRxiv : the preprint server for biology · 2025Article
- G4 Oligonucleotide-Based Chaperones of Heterogeneous Nuclear Ribonucleoprotein A1.International journal of molecular sciences · 2025Article
- Coding relationship links RNA G-quadruplexes and protein RGG motifs in RNA-binding protein autoregulation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
RNA G-quadruplexes (rG4s), the four-stranded structures formed by guanine-rich RNA sequences, are recognized by regions in RNA-binding proteins (RBPs) that are enriched in arginine-glycine repeats (RGG motifs). Importantly, arginine and glycine are encoded by guanine-rich codons, suggesting that some RGG motifs may both be encoded by and interact with rG4s in autogenous messenger RNAs (mRNAs). By analyzing transcriptome-wide rG4 datasets, we show that hundreds of RGG motifs in humans are at least partly encoded by rG4s, with an increased incidence for longer RGG motifs (~10 or more residues). Using randomized genetic codes, we demonstrate that the rG4/RGG coding relationship derives from the universal genetic code's structure. Moreover, we show that proteins, which contain RGG motifs encoded by experimentally detected rG4s, are significantly enriched in RNA binding relative to all RGG-containing proteins. Finally, using enhanced crosslinking and immunoprecipitation (eCLIP) data, we identify several prominent RBPs, including FUS, FMRP, and G3BP1, which interact with autogenous mRNAs in regions where RGG motifs are encoded by rG4s. Our results define a physically realistic mechanism behind autogenous mRNA/protein interactions that is hardwired in the genetic code structure and may contribute to the establishment of autoregulatory feedback loops in the cell.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.