7o6u

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the VIN3 VEL polymerising domain (R554A R556D mutant)

Structural highlights

7o6u is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.84Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VIN3_ARATH Plays a central role in vernalization by mediating the initial transcriptional repression of the homeotic gene FLC, a floral repressor, after a cold treatment. However, due to its transient expression, it cannot maintain repression of FLC, which is then maintained by Polycomb Group complexes containing VRN2 throughout development. Required to deacetylate histones on the FLC promoter. Together with VIL1, required during vernalization for the modifications of FLC and FLM chromatin that are associated with an epigenetically silenced state (e.g. chromatin modifications, histone deacetylation, and trimethylated H3 'Lys-4' H3K4me3 and 'Lys-27' H3K27me3) and with acquisition of competence to flower.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Transcriptional silencing through the Polycomb silencing machinery utilizes a "read-write" mechanism involving histone tail modifications. However, nucleation of silencing and long-term stable transmission of the silenced state also requires P-olycomb Repressive Complex 2 (PRC2) accessory proteins, whose molecular role is poorly understood. The Arabidopsis VEL proteins are accessory proteins that interact with PRC2 to nucleate and propagate silencing at the FLOWERING LOCUS C (FLC) locus, enabling early flowering in spring. Here, we report that VEL proteins contain a domain related to an atypical four-helix bundle that engages in spontaneous concentration-dependent head-to-tail polymerization to assemble dynamic biomolecular condensates. Mutations blocking polymerization of this VEL domain prevent Polycomb silencing at FLC. Plant VEL proteins thus facilitate assembly of dynamic multivalent Polycomb complexes required for inheritance of the silenced state.

Head-to-tail polymerization by VEL proteins underpins cold-induced Polycomb silencing in flowering control.,Fiedler M, Franco-Echevarria E, Schulten A, Nielsen M, Rutherford TJ, Yeates A, Ahsan B, Dean C, Bienz M Cell Rep. 2022 Nov 8;41(6):111607. doi: 10.1016/j.celrep.2022.111607. PMID:36351412^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sung S, Amasino RM. Vernalization in Arabidopsis thaliana is mediated by the PHD finger protein VIN3. Nature. 2004 Jan 8;427(6970):159-64. PMID:14712276 doi:http://dx.doi.org/10.1038/nature02195
↑ Sung S, Schmitz RJ, Amasino RM. A PHD finger protein involved in both the vernalization and photoperiod pathways in Arabidopsis. Genes Dev. 2006 Dec 1;20(23):3244-8. doi: 10.1101/gad.1493306. Epub 2006 Nov 17. PMID:17114575 doi:http://dx.doi.org/10.1101/gad.1493306
↑ Greb T, Mylne JS, Crevillen P, Geraldo N, An H, Gendall AR, Dean C. The PHD finger protein VRN5 functions in the epigenetic silencing of Arabidopsis FLC. Curr Biol. 2007 Jan 9;17(1):73-8. Epub 2006 Dec 14. PMID:17174094 doi:http://dx.doi.org/S0960-9822(06)02570-X
↑ Fiedler M, Franco-Echevarría E, Schulten A, Nielsen M, Rutherford TJ, Yeates A, Ahsan B, Dean C, Bienz M. Head-to-tail polymerization by VEL proteins underpins cold-induced Polycomb silencing in flowering control. Cell Rep. 2022 Nov 8;41(6):111607. PMID:36351412 doi:10.1016/j.celrep.2022.111607

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7o6u"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7o6u is ON HOLD  until Paper Publication
+==Crystal structure of the VIN3 VEL polymerising domain (R554A R556D mutant)==
+<StructureSection load='7o6u' size='340' side='right'caption='[[7o6u]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7o6u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O6U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O6U FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.84&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=7o6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o6u OCA], [https://pdbe.org/7o6u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o6u RCSB], [https://www.ebi.ac.uk/pdbsum/7o6u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o6u ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/VIN3_ARATH VIN3_ARATH] Plays a central role in vernalization by mediating the initial transcriptional repression of the homeotic gene FLC, a floral repressor, after a cold treatment. However, due to its transient expression, it cannot maintain repression of FLC, which is then maintained by Polycomb Group complexes containing VRN2 throughout development. Required to deacetylate histones on the FLC promoter. Together with VIL1, required during vernalization for the modifications of FLC and FLM chromatin that are associated with an epigenetically silenced state (e.g. chromatin modifications, histone deacetylation, and trimethylated H3 'Lys-4' H3K4me3 and 'Lys-27' H3K27me3) and with acquisition of competence to flower.<ref>PMID:14712276</ref> <ref>PMID:17114575</ref> <ref>PMID:17174094</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Transcriptional silencing through the Polycomb silencing machinery utilizes a "read-write" mechanism involving histone tail modifications. However, nucleation of silencing and long-term stable transmission of the silenced state also requires P-olycomb Repressive Complex 2 (PRC2) accessory proteins, whose molecular role is poorly understood. The Arabidopsis VEL proteins are accessory proteins that interact with PRC2 to nucleate and propagate silencing at the FLOWERING LOCUS C (FLC) locus, enabling early flowering in spring. Here, we report that VEL proteins contain a domain related to an atypical four-helix bundle that engages in spontaneous concentration-dependent head-to-tail polymerization to assemble dynamic biomolecular condensates. Mutations blocking polymerization of this VEL domain prevent Polycomb silencing at FLC. Plant VEL proteins thus facilitate assembly of dynamic multivalent Polycomb complexes required for inheritance of the silenced state.
-Authors:
+Head-to-tail polymerization by VEL proteins underpins cold-induced Polycomb silencing in flowering control.,Fiedler M, Franco-Echevarria E, Schulten A, Nielsen M, Rutherford TJ, Yeates A, Ahsan B, Dean C, Bienz M Cell Rep. 2022 Nov 8;41(6):111607. doi: 10.1016/j.celrep.2022.111607. PMID:36351412<ref>PMID:36351412</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7o6u" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Arabidopsis thaliana]]
+[[Category: Large Structures]]
+[[Category: Bienz M]]
+[[Category: Dean C]]
+[[Category: Fiedler M]]
+[[Category: Franco-Echevarria E]]

7o6u

From Proteopedia

Current revision

Crystal structure of the VIN3 VEL polymerising domain (R554A R556D mutant)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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