7t7t
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==Structure of TSK/BRU1 bound to histone H3.1== |
| - | <StructureSection load='7t7t' size='340' side='right'caption='[[7t7t]]' scene=''> | + | <StructureSection load='7t7t' size='340' side='right'caption='[[7t7t]], [[Resolution|resolution]] 3.17Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7t7t]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] and [https://en.wikipedia.org/wiki/Citrus_unshiu Citrus unshiu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7T7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7T7T FirstGlance]. <br> |
| - | </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=7t7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7t7t OCA], [https://pdbe.org/7t7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7t7t RCSB], [https://www.ebi.ac.uk/pdbsum/7t7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7t7t ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.17Å</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=7t7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7t7t OCA], [https://pdbe.org/7t7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7t7t RCSB], [https://www.ebi.ac.uk/pdbsum/7t7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7t7t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TONSL_CITUN TONSL_CITUN] Histone reader involved in homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks (By similarity). Specifically recognizes and binds histone H3.1 lacking methylation at 'Lys-27' (H3K27me1) (PubMed:35298257).[UniProtKB:Q6Q4D0]<ref>PMID:35298257</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The tail of replication-dependent histone H3.1 varies from that of replication-independent H3.3 at the amino acid located at position 31 in plants and animals, but no function has been assigned to this residue to demonstrate a unique and conserved role for H3.1 during replication. We found that TONSOKU (TSK/TONSL), which rescues broken replication forks, specifically interacts with H3.1 via recognition of alanine 31 by its tetratricopeptide repeat domain. Our results indicate that genomic instability in the absence of ATXR5/ATXR6-catalyzed histone H3 lysine 27 monomethylation in plants depends on H3.1, TSK, and DNA polymerase theta (Pol theta). This work reveals an H3.1-specific function during replication and a common strategy used in multicellular eukaryotes for regulating post-replicative chromatin maturation and TSK, which relies on histone monomethyltransferases and reading of the H3.1 variant. | ||
| + | |||
| + | The histone H3.1 variant regulates TONSOKU-mediated DNA repair during replication.,Davarinejad H, Huang YC, Mermaz B, LeBlanc C, Poulet A, Thomson G, Joly V, Munoz M, Arvanitis-Vigneault A, Valsakumar D, Villarino G, Ross A, Rotstein BH, Alarcon EI, Brunzelle JS, Voigt P, Dong J, Couture JF, Jacob Y Science. 2022 Mar 18;375(6586):1281-1286. doi: 10.1126/science.abm5320. Epub 2022 , Mar 17. PMID:35298257<ref>PMID:35298257</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7t7t" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Arabidopsis thaliana]] | ||
| + | [[Category: Citrus unshiu]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Couture JF]] |
| + | [[Category: Davarinejad H]] | ||
Current revision
Structure of TSK/BRU1 bound to histone H3.1
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