6fas

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Current revision (07:56, 17 October 2024) (edit) (undo)
 
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6fas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fas OCA], [https://pdbe.org/6fas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fas RCSB], [https://www.ebi.ac.uk/pdbsum/6fas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fas ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6fas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fas OCA], [https://pdbe.org/6fas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fas RCSB], [https://www.ebi.ac.uk/pdbsum/6fas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fas ProSAT]</span></td></tr>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/VAL1_ARATH VAL1_ARATH] Transcriptional repressor of gene expression involved in embryonic pathways, such as LEC1, ABI3, and FUS3. Repressor of the sugar-inducible genes involved in the seed maturation program in seedlings. Plays an essential role in regulating the transition from seed maturation to seedling growth. Functionally redundant with VAL2/HSL1.<ref>PMID:15894743</ref> <ref>PMID:17158584</ref> <ref>PMID:17267611</ref>
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== Publication Abstract from PubMed ==
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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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Structural basis of DNA target recognition by the B3 domain of Arabidopsis epigenome reader VAL1.,Sasnauskas G, Kauneckaite K, Siksnys V Nucleic Acids Res. 2018 Apr 6. pii: 4962483. doi: 10.1093/nar/gky256. PMID:29660015<ref>PMID:29660015</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6fas" style="background-color:#fffaf0;"></div>
== References ==
== References ==
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Current revision

Crystal structure of VAL1 B3 domain in complex with cognate DNA

PDB ID 6fas

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