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| | ==Structure of Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate.== | | ==Structure of Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate.== |
| - | <StructureSection load='6o22' size='340' side='right'caption='[[6o22]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | + | <StructureSection load='6o22' size='340' side='right'caption='[[6o22]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6o22]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog] and [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6O22 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6o22]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O22 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VPS75, YNL246W, N0890 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RTT109, KIM2, REM50, YLL002W, L1377 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), ASF1, CIA1, YJL115W, J0755 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Hybrid , Solution NMR , X-ray solution scattering</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </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=6o22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o22 OCA], [https://pdbe.org/6o22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o22 RCSB], [https://www.ebi.ac.uk/pdbsum/6o22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o22 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6o22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o22 OCA], [http://pdbe.org/6o22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o22 RCSB], [http://www.ebi.ac.uk/pdbsum/6o22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o22 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/H32_XENLA H32_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [[http://www.uniprot.org/uniprot/VPS75_YEAST VPS75_YEAST]] Histone chaperone which acts as a cofactor stimulating the histone H3 'Lys-56' acetylation by RTT109. May be involved in vacuolar proteins sorting.<ref>PMID:12134085</ref> <ref>PMID:17320445</ref> [[http://www.uniprot.org/uniprot/ASF1_YEAST ASF1_YEAST]] Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Facilitates histone deposition through both replication-dependent and replication-independent chromatin assembly pathways. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with the HIR complex to promote replication-independent chromatin assembly, which may occur during transcription and DNA repair. May be required for the maintenance of a subset of replication elongation factors, including DNA polymerase epsilon, the RFC complex and PCNA, at stalled replication forks. Also required for acetylation of histone H3 on 'Lys-9' and 'Lys-56'.<ref>PMID:9290207</ref> <ref>PMID:10591219</ref> <ref>PMID:11412995</ref> <ref>PMID:11331602</ref> <ref>PMID:11731479</ref> <ref>PMID:11731480</ref> <ref>PMID:11404324</ref> <ref>PMID:11172707</ref> <ref>PMID:11856374</ref> <ref>PMID:11756556</ref> <ref>PMID:12093919</ref> <ref>PMID:14585955</ref> <ref>PMID:15071494</ref> <ref>PMID:15452122</ref> <ref>PMID:15175160</ref> <ref>PMID:15542829</ref> <ref>PMID:15542840</ref> <ref>PMID:15766286</ref> <ref>PMID:16303565</ref> <ref>PMID:15821127</ref> <ref>PMID:15901673</ref> <ref>PMID:16020781</ref> <ref>PMID:16143623</ref> <ref>PMID:16039596</ref> <ref>PMID:15632066</ref> <ref>PMID:15891116</ref> <ref>PMID:16141196</ref> <ref>PMID:15840725</ref> <ref>PMID:16815704</ref> <ref>PMID:16936140</ref> <ref>PMID:16582440</ref> <ref>PMID:16407267</ref> <ref>PMID:17046836</ref> <ref>PMID:16678113</ref> <ref>PMID:16501045</ref> <ref>PMID:16627621</ref> <ref>PMID:17107956</ref> <ref>PMID:17320445</ref> <ref>PMID:14680630</ref> [[http://www.uniprot.org/uniprot/RT109_YEAST RT109_YEAST]] Required for acetylation of 'Lys-56' of histone H3 (H3K56ac) which occurs in S phase and disappears during G(2)/M phase of the cell cycle and is involved in transcription DNA repair process. H3K56 acetylation weakens of the interaction between the histone core and the surrounding DNA in the nucleosomal particle and drives chromatin disassembly. Involved in regulation of Ty1 transposition.<ref>PMID:11779788</ref> <ref>PMID:17046836</ref> <ref>PMID:17369253</ref> <ref>PMID:17690098</ref> <ref>PMID:17320445</ref> <ref>PMID:17272722</ref> <ref>PMID:17272723</ref> <ref>PMID:18577595</ref> <ref>PMID:18723682</ref> [[http://www.uniprot.org/uniprot/H4_XENLA H4_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | + | [https://www.uniprot.org/uniprot/VPS75_YEAST VPS75_YEAST] Histone chaperone which acts as a cofactor stimulating the histone H3 'Lys-56' acetylation by RTT109. May be involved in vacuolar proteins sorting.<ref>PMID:12134085</ref> <ref>PMID:17320445</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Histones, the principal protein components of chromatin, contain long disordered sequences, which are extensively post-translationally modified. Although histone chaperones are known to control both the activity and specificity of histone-modifying enzymes, the mechanisms promoting modification of highly disordered substrates, such as lysine-acetylation within the N-terminal tail of histone H3, are not understood. Here, to understand how histone chaperones Asf1 and Vps75 together promote H3 K9-acetylation, we establish the solution structural model of the acetyltransferase Rtt109 in complex with Asf1 and Vps75 and the histone dimer H3:H4. We show that Vps75 promotes K9-acetylation by engaging the H3 N-terminal tail in fuzzy electrostatic interactions with its disordered C-terminal domain, thereby confining the H3 tail to a wide central cavity faced by the Rtt109 active site. These fuzzy interactions between disordered domains achieve localization of lysine residues in the H3 tail to the catalytic site with minimal loss of entropy, and may represent a common mechanism of enzymatic reactions involving highly disordered substrates.
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| - | Histone chaperone exploits intrinsic disorder to switch acetylation specificity.,Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T Nat Commun. 2019 Aug 6;10(1):3435. doi: 10.1038/s41467-019-11410-7. PMID:31387991<ref>PMID:31387991</ref>
| + | ==See Also== |
| - | | + | *[[Anti-silencing factor 3D structures|Anti-silencing factor 3D structures]] |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | *[[Histone 3D structures|Histone 3D structures]] |
| - | </div>
| + | *[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]] |
| - | <div class="pdbe-citations 6o22" style="background-color:#fffaf0;"></div>
| + | *[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: African clawed frog]] | |
| - | [[Category: Baker's yeast]] | |
| - | [[Category: Histone acetyltransferase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Carlomagno, T]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Danilenko, N]] | + | [[Category: Xenopus laevis]] |
| - | [[Category: Kirkpatrick, J P]] | + | [[Category: Carlomagno T]] |
| - | [[Category: Chaperone]] | + | [[Category: Danilenko N]] |
| | + | [[Category: Kirkpatrick JP]] |
