ArticleThe Journal of biological chemistry2014
Structure of Yin Yang 1 oligomers that cooperate with RuvBL1-RuvBL2 ATPases.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
31 citing papers in PubMed, 50 citations in OpenAlex.
- Insight into meiotic DNA end resection: Mechanisms and regulation.DNA repair · 2025Review
- YY1 mutations disrupt corticogenesis through a cell type specific rewiring of cell-autonomous and non-cell-autonomous transcriptional programs.Molecular psychiatry · 2025Article
- Expression of foetal gene Pontin is essential in protecting heart against pathological remodelling and cardiomyopathy.Nature communications · 2025Article
- Yin Yang 1: Function, Mechanisms, and Glia.Neurochemical research · 2025Review
- YY1 is a transcriptional activator of the mouse LINE-1 Tf subfamily.Nucleic acids research · 2024Article
- YY1-controlled regulatory connectivity and transcription are influenced by the cell cycle.Nature genetics · 2024Article
- YY1 mutations disrupt corticogenesis through a cell-type specific rewiring of cell-autonomous and non-cell-autonomous transcriptional programs.bioRxiv : the preprint server for biology · 2024Article
- YY1 is a transcriptional activator of mouse LINE-1 Tf subfamily.bioRxiv : the preprint server for biology · 2024Article
- Assessing the dynamics and macromolecular interactions of the intrinsically disordered protein YY1.Bioscience reports · 2023Article
- Review
- The Role of Protein Arginine Methyltransferases in DNA Damage Response.International journal of molecular sciences · 2022Review
- Coming full circle: On the origin and evolution of the looping model for enhancer-promoter communication.The Journal of biological chemistry · 2022Review
- A histidine cluster determines YY1-compartmentalized coactivators and chromatin elements in phase-separated enhancer clusters.Nucleic acids research · 2022Article
- YY1 Oligomerization Is Regulated by Its OPB Domain and Competes with Its Regulation of Oncoproteins.Cancers · 2022Article
- CryoEM of RUVBL1-RUVBL2-ZNHIT2, a complex that interacts with pre-mRNA-processing-splicing factor 8.Nucleic acids research · 2022Article
- Mechanisms of enhancer-promoter communication and chromosomal architecture in mammals andFrontiers in genetics · 2022Review
- YY1 interacts with guanine quadruplexes to regulate DNA looping and gene expression.Nature chemical biology · 2021Article
- Mechanisms of Enhancer-Promoter Interactions in Higher Eukaryotes.International journal of molecular sciences · 2021Review
- 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
- N-terminal domain of the architectural protein CTCF has similar structural organization and ability to self-association in bilaterian organisms.Scientific reports · 2020Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Yin Yang 1 (YY1) is a transcription factor regulating proliferation and differentiation and is involved in cancer development. Oligomers of recombinant YY1 have been observed before, but their structure and DNA binding properties are not well understood. Here we find that YY1 assembles several homo-oligomeric species built from the association of a bell-shaped dimer, a process we characterized by electron microscopy. Moreover, we find that YY1 self-association also occurs in vivo using bimolecular fluorescence complementation. Unexpectedly, these oligomers recognize several DNA substrates without the consensus sequence for YY1 in vitro, and DNA binding is enhanced in the presence of RuvBL1-RuvBL2, two essential AAA+ ATPases. YY1 oligomers bind RuvBL1-RuvBL2 hetero-oligomeric complexes, but YY1 interacts preferentially with RuvBL1. Collectively, these findings suggest that YY1-RuvBL1-RuvBL2 complexes could contribute to functions beyond transcription, and we show that YY1 and the ATPase activity of RuvBL2 are required for RAD51 foci formation during homologous recombination.
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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.