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| - | [[Image:2i32.gif|left|200px]]<br /> | |
| - | <applet load="2i32" size="450" color="white" frame="true" align="right" spinBox="true" | |
| - | caption="2i32, resolution 2.700Å" /> | |
| - | '''Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly'''<br /> | |
| | | | |
| - | ==Overview== | + | ==Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly== |
| - | Human HIRA, ASF1a, ASF1b and CAF-1 are evolutionally conserved histone, chaperones that form multiple functionally distinct chromatin-assembly, complexes, with roles linked to diverse nuclear process, such as DNA, replication and formation of heterochromatin in senescent cells. We report, the crystal structure of an ASF1a-HIRA heterodimer and a biochemical, dissection of ASF1a's mutually exclusive interactions with HIRA and the, p60 subunit of CAF-1. The HIRA B domain forms an antiparallel beta-hairpin, that binds perpendicular to the strands of the beta-sandwich of ASF1a, via, beta-sheet, salt bridge and van der Waals contacts. The N- and C-terminal, regions of ASF1a and ASF1b determine the different affinities of these two, proteins for HIRA, by contacting regions outside the HIRA B domain. CAF-1, p60 also uses B domain-like motifs for binding to ASF1a, thereby competing, with HIRA. Together, these studies begin to define the molecular, determinants of assembly of functionally diverse macromolecular histone, chaperone complexes. | + | <StructureSection load='2i32' size='340' side='right'caption='[[2i32]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | + | == Structural highlights == |
| | + | <table><tr><td colspan='2'>[[2i32]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I32 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]] 2.7Å</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=2i32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i32 OCA], [https://pdbe.org/2i32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i32 RCSB], [https://www.ebi.ac.uk/pdbsum/2i32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i32 ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ASF1A_HUMAN ASF1A_HUMAN] Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit.<ref>PMID:10759893</ref> <ref>PMID:11897662</ref> <ref>PMID:12842904</ref> <ref>PMID:14718166</ref> <ref>PMID:15621527</ref> <ref>PMID:16151251</ref> <ref>PMID:15664198</ref> |
| | + | == Evolutionary Conservation == |
| | + | [[Image:Consurf_key_small.gif|200px|right]] |
| | + | Check<jmol> |
| | + | <jmolCheckbox> |
| | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i3/2i32_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | + | <text>to colour the structure by Evolutionary Conservation</text> |
| | + | </jmolCheckbox> |
| | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2i32 ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | Human HIRA, ASF1a, ASF1b and CAF-1 are evolutionally conserved histone chaperones that form multiple functionally distinct chromatin-assembly complexes, with roles linked to diverse nuclear process, such as DNA replication and formation of heterochromatin in senescent cells. We report the crystal structure of an ASF1a-HIRA heterodimer and a biochemical dissection of ASF1a's mutually exclusive interactions with HIRA and the p60 subunit of CAF-1. The HIRA B domain forms an antiparallel beta-hairpin that binds perpendicular to the strands of the beta-sandwich of ASF1a, via beta-sheet, salt bridge and van der Waals contacts. The N- and C-terminal regions of ASF1a and ASF1b determine the different affinities of these two proteins for HIRA, by contacting regions outside the HIRA B domain. CAF-1 p60 also uses B domain-like motifs for binding to ASF1a, thereby competing with HIRA. Together, these studies begin to define the molecular determinants of assembly of functionally diverse macromolecular histone chaperone complexes. |
| | | | |
| - | ==About this Structure==
| + | Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly.,Tang Y, Poustovoitov MV, Zhao K, Garfinkel M, Canutescu A, Dunbrack R, Adams PD, Marmorstein R Nat Struct Mol Biol. 2006 Oct;13(10):921-9. Epub 2006 Sep 17. PMID:16980972<ref>PMID:16980972</ref> |
| - | 2I32 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2I32 OCA].
| + | |
| | | | |
| - | ==Reference==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly., Tang Y, Poustovoitov MV, Zhao K, Garfinkel M, Canutescu A, Dunbrack R, Adams PD, Marmorstein R, Nat Struct Mol Biol. 2006 Oct;13(10):921-9. Epub 2006 Sep 17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16980972 16980972]
| + | </div> |
| - | [[Category: Homo sapiens]]
| + | <div class="pdbe-citations 2i32" style="background-color:#fffaf0;"></div> |
| - | [[Category: Protein complex]]
| + | |
| - | [[Category: Marmorstein, R.]]
| + | |
| - | [[Category: Tang, Y.]]
| + | |
| - | [[Category: asf1]]
| + | |
| - | [[Category: caf-1]]
| + | |
| - | [[Category: chromatin regulation]]
| + | |
| - | [[Category: hira]]
| + | |
| - | [[Category: histone chaperones]]
| + | |
| - | [[Category: histone deposition]]
| + | |
| | | | |
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:40:05 2007''
| + | ==See Also== |
| | + | *[[Anti-silencing factor 3D structures|Anti-silencing factor 3D structures]] |
| | + | == References == |
| | + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | + | [[Category: Large Structures]] |
| | + | [[Category: Marmorstein R]] |
| | + | [[Category: Tang Y]] |
| Structural highlights
Function
ASF1A_HUMAN Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit.[1] [2] [3] [4] [5] [6] [7]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Human HIRA, ASF1a, ASF1b and CAF-1 are evolutionally conserved histone chaperones that form multiple functionally distinct chromatin-assembly complexes, with roles linked to diverse nuclear process, such as DNA replication and formation of heterochromatin in senescent cells. We report the crystal structure of an ASF1a-HIRA heterodimer and a biochemical dissection of ASF1a's mutually exclusive interactions with HIRA and the p60 subunit of CAF-1. The HIRA B domain forms an antiparallel beta-hairpin that binds perpendicular to the strands of the beta-sandwich of ASF1a, via beta-sheet, salt bridge and van der Waals contacts. The N- and C-terminal regions of ASF1a and ASF1b determine the different affinities of these two proteins for HIRA, by contacting regions outside the HIRA B domain. CAF-1 p60 also uses B domain-like motifs for binding to ASF1a, thereby competing with HIRA. Together, these studies begin to define the molecular determinants of assembly of functionally diverse macromolecular histone chaperone complexes.
Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly.,Tang Y, Poustovoitov MV, Zhao K, Garfinkel M, Canutescu A, Dunbrack R, Adams PD, Marmorstein R Nat Struct Mol Biol. 2006 Oct;13(10):921-9. Epub 2006 Sep 17. PMID:16980972[8]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Munakata T, Adachi N, Yokoyama N, Kuzuhara T, Horikoshi M. A human homologue of yeast anti-silencing factor has histone chaperone activity. Genes Cells. 2000 Mar;5(3):221-33. PMID:10759893
- ↑ Mello JA, Sillje HH, Roche DM, Kirschner DB, Nigg EA, Almouzni G. Human Asf1 and CAF-1 interact and synergize in a repair-coupled nucleosome assembly pathway. EMBO Rep. 2002 Apr;3(4):329-34. Epub 2002 Mar 15. PMID:11897662 doi:10.1093/embo-reports/kvf068
- ↑ Umehara T, Horikoshi M. Transcription initiation factor IID-interactive histone chaperone CIA-II implicated in mammalian spermatogenesis. J Biol Chem. 2003 Sep 12;278(37):35660-7. Epub 2003 Jul 2. PMID:12842904 doi:10.1074/jbc.M303549200
- ↑ Tagami H, Ray-Gallet D, Almouzni G, Nakatani Y. Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis. Cell. 2004 Jan 9;116(1):51-61. PMID:14718166
- ↑ Zhang R, Poustovoitov MV, Ye X, Santos HA, Chen W, Daganzo SM, Erzberger JP, Serebriiskii IG, Canutescu AA, Dunbrack RL, Pehrson JR, Berger JM, Kaufman PD, Adams PD. Formation of MacroH2A-containing senescence-associated heterochromatin foci and senescence driven by ASF1a and HIRA. Dev Cell. 2005 Jan;8(1):19-30. PMID:15621527 doi:S1534580704004083
- ↑ Tamburini BA, Carson JJ, Adkins MW, Tyler JK. Functional conservation and specialization among eukaryotic anti-silencing function 1 histone chaperones. Eukaryot Cell. 2005 Sep;4(9):1583-90. PMID:16151251 doi:10.1128/EC.4.9.1583-1590.2005
- ↑ Groth A, Ray-Gallet D, Quivy JP, Lukas J, Bartek J, Almouzni G. Human Asf1 regulates the flow of S phase histones during replicational stress. Mol Cell. 2005 Jan 21;17(2):301-11. PMID:15664198 doi:S1097276504008020
- ↑ Tang Y, Poustovoitov MV, Zhao K, Garfinkel M, Canutescu A, Dunbrack R, Adams PD, Marmorstein R. Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly. Nat Struct Mol Biol. 2006 Oct;13(10):921-9. Epub 2006 Sep 17. PMID:16980972 doi:10.1038/nsmb1147
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