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2iij

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Revision as of 11:16, 31 March 2021

Structure of human Asf1a in complex with histone H3

Structural highlights

2iij is a 2 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1tey
Gene:	ASF1A (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Asf1 is a histone chaperone that favors histone H3/H4 assembly and disassembly. We solved the structure of the conserved domain of human ASF1A in complex with the C-terminal helix of histone H3 using nuclear magnetic resonance spectroscopy. This structure is fully compatible with an association of ASF1 with the heterodimeric form of histones H3/H4. In our model, ASF1 substitutes for the second H3/H4 heterodimer that is normally found in heterotetrameric H3/H4 complexes. This result constitutes an essential step in the fundamental understanding of the mechanisms of nucleosome assembly by histone chaperones. Point mutations that perturb the Asf1/histone interface were designed from the structure. The decreased binding affinity of the Asf1-H3/H4 complex correlates with decreased levels of H3-K56 acetylation and phenotypic defects in vivo.

Structure of the histone chaperone ASF1 bound to the histone H3 C-terminal helix and functional insights.,Agez M, Chen J, Guerois R, van Heijenoort C, Thuret JY, Mann C, Ochsenbein F Structure. 2007 Feb;15(2):191-9. PMID:17292837^[8]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
↑ Agez M, Chen J, Guerois R, van Heijenoort C, Thuret JY, Mann C, Ochsenbein F. Structure of the histone chaperone ASF1 bound to the histone H3 C-terminal helix and functional insights. Structure. 2007 Feb;15(2):191-9. PMID:17292837 doi:10.1016/j.str.2007.01.002

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2iij"

@@ Line 1: / Line 1: @@
 ==Structure of human Asf1a in complex with histone H3==
-<StructureSection load='2iij' size='340' side='right' caption='[[2iij]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2iij' size='340' side='right'caption='[[2iij]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2iij]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IIJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IIJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2iij]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IIJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IIJ FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tey|1tey]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1tey|1tey]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ASF1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ASF1A ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2iij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iij OCA], [http://pdbe.org/2iij PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iij RCSB], [http://www.ebi.ac.uk/pdbsum/2iij PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2iij 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=2iij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iij OCA], [https://pdbe.org/2iij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iij RCSB], [https://www.ebi.ac.uk/pdbsum/2iij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iij ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[[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]]
@@ Line 29: / Line 29: @@
 </div>
 <div class="pdbe-citations 2iij" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Anti-silencing factor 3D structures|Anti-silencing factor 3D structures]]
 == References ==
 <references/>
@@ Line 34: / Line 37: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Agez, M]]
 [[Category: Guerois, R]]

2iij

From Proteopedia

Revision as of 11:16, 31 March 2021

Structure of human Asf1a in complex with histone H3

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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