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| | ==SPT16-H2A-H2B FACT HISTONE Complex== | | ==SPT16-H2A-H2B FACT HISTONE Complex== |
| - | <StructureSection load='4wnn' size='340' side='right' caption='[[4wnn]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='4wnn' size='340' side='right'caption='[[4wnn]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4wnn]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WNN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WNN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4wnn]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WNN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WNN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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]] 1.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HTA1, H2A1, SPT11, YDR225W, YD9934.10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), HTB1, H2B1, SPT12, YDR224C, YD9934.09C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=4wnn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wnn OCA], [http://pdbe.org/4wnn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wnn RCSB], [http://www.ebi.ac.uk/pdbsum/4wnn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wnn 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=4wnn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wnn OCA], [https://pdbe.org/4wnn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wnn RCSB], [https://www.ebi.ac.uk/pdbsum/4wnn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wnn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/H2A1_YEAST H2A1_YEAST]] Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. 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.<ref>PMID:11140636</ref> <ref>PMID:15458641</ref> <ref>PMID:15610741</ref> <ref>PMID:16299494</ref> [[http://www.uniprot.org/uniprot/H2B1_YEAST H2B1_YEAST]] 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.<ref>PMID:11973294</ref> <ref>PMID:12152067</ref> <ref>PMID:14752010</ref> <ref>PMID:15280549</ref> <ref>PMID:15652479</ref> <ref>PMID:15970663</ref> <ref>PMID:15632126</ref> <ref>PMID:15632065</ref> <ref>PMID:16598039</ref> | + | [https://www.uniprot.org/uniprot/H2A1_YEAST H2A1_YEAST] Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. 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.<ref>PMID:11140636</ref> <ref>PMID:15458641</ref> <ref>PMID:15610741</ref> <ref>PMID:16299494</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4wnn" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4wnn" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Histone 3D structures|Histone 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | + | [[Category: Large Structures]] |
| - | [[Category: Baker's yeast]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Formosa, T]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Hill, C P]] | + | [[Category: Formosa T]] |
| - | [[Category: Kemble, D J]] | + | [[Category: Hill CP]] |
| - | [[Category: McCullough, L L]] | + | [[Category: Kemble DJ]] |
| - | [[Category: Whitby, F G]] | + | [[Category: McCullough LL]] |
| - | [[Category: Dna binding protein]] | + | [[Category: Whitby FG]] |
| - | [[Category: Fact]]
| + | |
| - | [[Category: H2a]]
| + | |
| - | [[Category: H2b]]
| + | |
| - | [[Category: Histone]]
| + | |
| - | [[Category: Pob3]]
| + | |
| - | [[Category: Spt16]]
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| Structural highlights
Function
H2A1_YEAST Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. 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.[1] [2] [3] [4]
Publication Abstract from PubMed
FACT, a heterodimer of Spt16 and Pob3, is an essential histone chaperone. We show that the H2A-H2B binding activity that is central to FACT function resides in short acidic regions near the C termini of each subunit. Mutations throughout these regions affect binding and cause correlated phenotypes that range from mild to lethal, with the largest individual contributions unexpectedly coming from an aromatic residue and a nearby carboxylate residue within each domain. Spt16 and Pob3 bind overlapping sites on H2A-H2B, and Spt16-Pob3 heterodimers simultaneously bind two H2A-H2B dimers, the same stoichiometry as the components of a nucleosome. An Spt16:H2A-H2B crystal structure explains the biochemical and genetic data, provides a model for Pob3 binding, and implies a mechanism for FACT reorganization that we confirm biochemically. Moreover, unexpected similarity to binding of ANP32E and Swr1 with H2A.Z-H2B reveals that diverse H2A-H2B chaperones use common mechanisms of histone binding and regulating nucleosome functions.
FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs.,Kemble DJ, McCullough LL, Whitby FG, Formosa T, Hill CP Mol Cell. 2015 Oct 15;60(2):294-306. doi: 10.1016/j.molcel.2015.09.008. Epub 2015, Oct 8. PMID:26455391[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Downs JA, Lowndes NF, Jackson SP. A role for Saccharomyces cerevisiae histone H2A in DNA repair. Nature. 2000 Dec 21-28;408(6815):1001-4. PMID:11140636 doi:10.1038/35050000
- ↑ Shroff R, Arbel-Eden A, Pilch D, Ira G, Bonner WM, Petrini JH, Haber JE, Lichten M. Distribution and dynamics of chromatin modification induced by a defined DNA double-strand break. Curr Biol. 2004 Oct 5;14(19):1703-11. PMID:15458641 doi:10.1016/j.cub.2004.09.047
- ↑ Unal E, Arbel-Eden A, Sattler U, Shroff R, Lichten M, Haber JE, Koshland D. DNA damage response pathway uses histone modification to assemble a double-strand break-specific cohesin domain. Mol Cell. 2004 Dec 22;16(6):991-1002. PMID:15610741 doi:S1097276504007191
- ↑ Keogh MC, Kim JA, Downey M, Fillingham J, Chowdhury D, Harrison JC, Onishi M, Datta N, Galicia S, Emili A, Lieberman J, Shen X, Buratowski S, Haber JE, Durocher D, Greenblatt JF, Krogan NJ. A phosphatase complex that dephosphorylates gammaH2AX regulates DNA damage checkpoint recovery. Nature. 2006 Jan 26;439(7075):497-501. Epub 2005 Nov 20. PMID:16299494 doi:nature04384
- ↑ Kemble DJ, McCullough LL, Whitby FG, Formosa T, Hill CP. FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs. Mol Cell. 2015 Oct 15;60(2):294-306. doi: 10.1016/j.molcel.2015.09.008. Epub 2015, Oct 8. PMID:26455391 doi:http://dx.doi.org/10.1016/j.molcel.2015.09.008
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