ArticleNucleic acids research2016
The zinc fingers of YY1 bind single-stranded RNA with low sequence specificity.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 39 citations in OpenAlex.
- HBiochemistry · 2026Article
- Mutant huntingtin induces neuronal apoptosis via derepressing the non-canonical poly(A) polymerase PAPD5.Nature communications · 2025Article
- Mutant GGGGCC RNA prevents YY1 from binding to Fuzzy promoter which stimulates Wnt/β-catenin pathway in C9ALS/FTD.Nature communications · 2023Article
- Interplay between lncRNA RP11-367G18.1 variant 2 and YY1 plays a vital role in hypoxia-mediated gene expression and tumorigenesis.Cancer cell international · 2023Article
- Assessing the dynamics and macromolecular interactions of the intrinsically disordered protein YY1.Bioscience reports · 2023Article
- Review
- Article
- Enhancer RNAs step forward: new insights into enhancer function.Development (Cambridge, England) · 2022Article
- Dual Role of YY1 in HPV Life Cycle and Cervical Cancer Development.International journal of molecular sciences · 2022Review
- YY1 Is a Key Player in Melanoma Immunotherapy/Targeted Treatment Resistance.Frontiers in oncology · 2022Review
- Structural basis for recognition and regulation of arenavirus polymerase L by Z protein.Nature communications · 2021Article
- Yin Yang 1 is a potent activator of human T lymphotropic virus type 1 LTR-driven gene expression via RNA binding.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Interactome of vertebrate GAF/ThPOK reveals its diverse functions in gene regulation and DNA repair.Journal of biosciences · 2020Article
- The Why of YY1: Mechanisms of Transcriptional Regulation by Yin Yang 1.Frontiers in cell and developmental biology · 2020Review
- The glucocorticoid receptor DNA-binding domain recognizes RNA hairpin structures with high affinity.Nucleic acids research · 2019Article
- Conserved RNA binding activity of a Yin-Yang 1 homologue in the ova of the purple sea urchin Strongylocentrotus purpuratus.Scientific reports · 2018Article
- Expression, purification and DNA-binding properties of zinc finger domains of DOF proteins fromBioImpacts : BI · 2018Article
- Loss of Xist RNA from the inactive X during B cell development is restored in a dynamic YY1-dependent two-step process in activated B cells.PLoS genetics · 2017Article
- How do lncRNAs regulate transcription?Science advances · 2017Review
- Deciphering the DNA code for the function of the Drosophila polydactyl zinc finger protein Suppressor of Hairy-wing.Nucleic acids research · 2017Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Classical zinc fingers (ZFs) are traditionally considered to act as sequence-specific DNA-binding domains. More recently, classical ZFs have been recognised as potential RNA-binding modules, raising the intriguing possibility that classical-ZF transcription factors are involved in post-transcriptional gene regulation via direct RNA binding. To date, however, only one classical ZF-RNA complex, that involving TFIIIA, has been structurally characterised. Yin Yang-1 (YY1) is a multi-functional transcription factor involved in many regulatory processes, and binds DNA via four classical ZFs. Recent evidence suggests that YY1 also interacts with RNA, but the molecular nature of the interaction remains unknown. In the present work, we directly assess the ability of YY1 to bind RNA using in vitro assays. Systematic Evolution of Ligands by EXponential enrichment (SELEX) was used to identify preferred RNA sequences bound by the YY1 ZFs from a randomised library over multiple rounds of selection. However, a strong motif was not consistently recovered, suggesting that the RNA sequence selectivity of these domains is modest. YY1 ZF residues involved in binding to single-stranded RNA were identified by NMR spectroscopy and found to be largely distinct from the set of residues involved in DNA binding, suggesting that interactions between YY1 and ssRNA constitute a separate mode of nucleic acid binding. Our data are consistent with recent reports that YY1 can bind to RNA in a low-specificity, yet physiologically relevant manner.
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