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| | <StructureSection load='5bt1' size='340' side='right'caption='[[5bt1]], [[Resolution|resolution]] 2.62Å' scene=''> | | <StructureSection load='5bt1' size='340' side='right'caption='[[5bt1]], [[Resolution|resolution]] 2.62Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5bt1]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BT1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BT1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5bt1]] is a 4 chain structure with sequence from [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=5BT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BT1 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4nq0|4nq0]]</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]] 2.62Å</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=5bt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bt1 OCA], [http://pdbe.org/5bt1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bt1 RCSB], [http://www.ebi.ac.uk/pdbsum/5bt1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bt1 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=5bt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bt1 OCA], [https://pdbe.org/5bt1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bt1 RCSB], [https://www.ebi.ac.uk/pdbsum/5bt1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bt1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HIF1_YEAST HIF1_YEAST]] Histone H3 and H4 specific chaperone component of the nuclear histone acetyltransferase B (HAT-B) complex. Involved in chromatin assembly and telomere silencing.<ref>PMID:14761951</ref> <ref>PMID:15099519</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> [[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> | + | [https://www.uniprot.org/uniprot/HIF1_YEAST HIF1_YEAST] Histone H3 and H4 specific chaperone component of the nuclear histone acetyltransferase B (HAT-B) complex. Involved in chromatin assembly and telomere silencing.<ref>PMID:14761951</ref> <ref>PMID:15099519</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gao, Y]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Liu, H]] | + | [[Category: Gao Y]] |
| - | [[Category: Niu, L]] | + | [[Category: Liu H]] |
| - | [[Category: Teng, M]] | + | [[Category: Niu L]] |
| - | [[Category: Zhang, M]] | + | [[Category: Teng M]] |
| - | [[Category: Assembly]]
| + | [[Category: Zhang M]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Histone chaperone complex]]
| + | |
| - | [[Category: Nasp homolog]]
| + | |
| - | [[Category: Tpr]]
| + | |
| Structural highlights
Function
HIF1_YEAST Histone H3 and H4 specific chaperone component of the nuclear histone acetyltransferase B (HAT-B) complex. Involved in chromatin assembly and telomere silencing.[1] [2]
Publication Abstract from PubMed
Histone chaperones are critical for guiding specific post-transcriptional modifications of histones, safeguarding the histone deposition (or disassociation) of nucleosome (dis)assembly, and regulating chromatin structures to change gene activities. HAT1-interacting factor 1 (Hif1) has been reported to be an H3-H4 chaperone and to be involved in telomeric silencing and nucleosome (dis)assembly. However, the structural basis for the interaction of Hif1 with histones remains unknown. Here, we report the complex structure of Hif1 binding to H2A-H2B for uncovering the chaperone specificities of Hif1 on binding to both the H2A-H2B dimer and the H3-H4 tetramer. Our findings reveal that Hif1 interacts with the H2A-H2B dimer and the H3-H4 tetramer via distinct mechanisms, suggesting that Hif1 is a pivotal scaffold on alternate binding of H2A-H2B and H3-H4. These specificities are conserved features of the Sim3-Hif1-NASP interrupted tetratricopeptide repeat proteins, which provide clues for investigating their potential roles in nucleosome (dis)assembly.
Structural Insights into the Association of Hif1 with Histones H2A-H2B Dimer and H3-H4 Tetramer.,Zhang M, Liu H, Gao Y, Zhu Z, Chen Z, Zheng P, Xue L, Li J, Teng M, Niu L Structure. 2016 Oct 4;24(10):1810-1820. doi: 10.1016/j.str.2016.08.001. Epub 2016, Sep 8. PMID:27618665[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Poveda A, Pamblanco M, Tafrov S, Tordera V, Sternglanz R, Sendra R. Hif1 is a component of yeast histone acetyltransferase B, a complex mainly localized in the nucleus. J Biol Chem. 2004 Apr 16;279(16):16033-43. Epub 2004 Feb 3. PMID:14761951 doi:http://dx.doi.org/10.1074/jbc.M314228200
- ↑ Ai X, Parthun MR. The nuclear Hat1p/Hat2p complex: a molecular link between type B histone acetyltransferases and chromatin assembly. Mol Cell. 2004 Apr 23;14(2):195-205. PMID:15099519
- ↑ Zhang M, Liu H, Gao Y, Zhu Z, Chen Z, Zheng P, Xue L, Li J, Teng M, Niu L. Structural Insights into the Association of Hif1 with Histones H2A-H2B Dimer and H3-H4 Tetramer. Structure. 2016 Oct 4;24(10):1810-1820. doi: 10.1016/j.str.2016.08.001. Epub 2016, Sep 8. PMID:27618665 doi:http://dx.doi.org/10.1016/j.str.2016.08.001
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