ArticleNucleic acids research2018
Structural basis of DNA target recognition by the B3 domain of Arabidopsis epigenome reader VAL1.
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 18 papers.
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Who cites it
18 citing papers in PubMed.
- Retrograde signals control dynamic changes to the chromatin state at photosynthesis-associated loci.Nature communications · 2025Article
- The chromatin accessibility landscape during early maize seed development.The Plant journal : for cell and molecular biology · 2025Article
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- The missing part: the Archaeoglobus fulgidus Argonaute forms a functional heterodimer with an N-L1-L2 domain protein.Nucleic acids research · 2024Article
- Identification of the Genes Encoding B3 Domain-Containing Proteins Related to Vernalization ofGenes · 2022Article
- Interaction Analysis between theInternational journal of molecular sciences · 2022Article
- Roles of Polycomb complexes in regulating gene expression and chromatin structure in plants.Plant communications · 2022Review
- Phytochrome B triggers light-dependent chromatin remodelling through the PRC2-associated PHD finger protein VIL1.Nature plants · 2021Article
- TEM1 combinatorially binds toProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Genetic and Molecular Control of Somatic Embryogenesis.Plants (Basel, Switzerland) · 2021Review
- Dynamics of H3K27me3 Modification on Plant Adaptation to Environmental Cues.Plants (Basel, Switzerland) · 2021Review
- VAL genes regulate vegetative phase change via miR156-dependent and independent mechanisms.PLoS genetics · 2021Article
- Article
- Structural variation affecting DNA backbone interactions underlies adaptation of B3 DNA binding domains to constraints imposed by protein architecture.Nucleic acids research · 2021Article
- The transcriptional repressors VAL1 and VAL2 recruit PRC2 for genome-wide Polycomb silencing in Arabidopsis.Nucleic acids research · 2021Article
- Crystal structure of the EcoKMcrA N-terminal domain (NEco): recognition of modified cytosine bases without flipping.Nucleic acids research · 2019Article
- The B3-Domain Transcription Factor VAL1 Regulates the Floral Transition by RepressingPlant physiology · 2019Article
- Evolution and conservation of polycomb repressive complex 1 core components and putative associated factors in the green lineage.BMC genomics · 2019Article
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3 authors.
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Abstract
Arabidopsis thaliana requires a prolonged period of cold exposure during winter to initiate flowering in a process termed vernalization. Exposure to cold induces epigenetic silencing of the FLOWERING LOCUS C (FLC) gene by Polycomb group (PcG) proteins. A key role in this epigenetic switch is played by transcriptional repressors VAL1 and VAL2, which specifically recognize Sph/RY DNA sequences within FLC via B3 DNA binding domains, and mediate recruitment of PcG silencing machinery. To understand the structural mechanism of site-specific DNA recognition by VAL1, we have solved the crystal structure of VAL1 B3 domain (VAL1-B3) bound to a 12 bp oligoduplex containing the canonical Sph/RY DNA sequence 5'-CATGCA-3'/5'-TGCATG-3'. We find that VAL1-B3 makes H-bonds and van der Waals contacts to DNA bases of all six positions of the canonical Sph/RY element. In agreement with the structure, in vitro DNA binding studies show that VAL1-B3 does not tolerate substitutions at any position of the 5'-TGCATG-3' sequence. The VAL1-B3-DNA structure presented here provides a structural model for understanding the specificity of plant B3 domains interacting with the Sph/RY and other DNA sequences.
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