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6JNL

REF6 ZnF2-4-NAC004 complex

Summary for 6JNL
Entry DOI10.2210/pdb6jnl/pdb
DescriptorLysine-specific demethylase REF6, DNA (5'-D(*TP*TP*CP*TP*CP*TP*GP*TP*TP*TP*TP*G)-3'), DNA (5'-D(*CP*AP*AP*AP*AP*CP*AP*GP*AP*GP*A)-3'), ... (8 entities in total)
Functional Keywordsref6, zinc finger, 5mc, dna complex, dna binding protein-dna complex, dna binding protein/dna
Biological sourceArabidopsis thaliana (Mouse-ear cress)
More
Total number of polymer chains3
Total formula weight19679.58
Authors
Yao, Q.Q.,Wu, B.X.,Ma, J.B. (deposition date: 2019-03-17, release date: 2019-03-27, Last modification date: 2024-05-29)
Primary citationQiu, Q.,Mei, H.,Deng, X.,He, K.,Wu, B.,Yao, Q.,Zhang, J.,Lu, F.,Ma, J.,Cao, X.
DNA methylation repels targeting of Arabidopsis REF6.
Nat Commun, 10:2063-2063, 2019
Cited by
PubMed Abstract: RELATIVE OF EARLY FLOWERING 6 (REF6/JMJ12), a Jumonji C (JmjC)-domain-containing H3K27me3 histone demethylase, finds its target loci in Arabidopsis genome by directly recognizing the CTCTGYTY motif via its zinc-finger (ZnF) domains. REF6 tends to bind motifs located in active chromatin states that are depleted for heterochromatic modifications. However, the underlying mechanism remains unknown. Here, we show that REF6 preferentially bind to hypo-methylated CTCTGYTY motifs in vivo, and that CHG methylation decreases REF6 DNA binding affinity in vitro. In addition, crystal structures of ZnF-clusters in complex with DNA oligonucleotides reveal that 5-methylcytosine is unfavorable for REF6 binding. In drm1 drm2 cmt2 cmt3 (ddcc) quadruple mutants, in which non-CG methylation is significantly reduced, REF6 can ectopically bind a small number of new target loci, most of which are located in or neighbored with short TEs in euchromatic regions. Collectively, our findings reveal that DNA methylation, likely acting in combination with other epigenetic modifications, may partially explain why REF6 binding is depleted in heterochromatic loci.
PubMed: 31048693
DOI: 10.1038/s41467-019-10026-1
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.15 Å)
Structure validation

245663

数据于2025-12-03公开中

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