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| | ==Structure of the Nap1 H2A H2B complex== | | ==Structure of the Nap1 H2A H2B complex== |
| - | <StructureSection load='5g2e' size='340' side='right' caption='[[5g2e]], [[Resolution|resolution]] 6.70Å' scene=''> | + | <StructureSection load='5g2e' size='340' side='right'caption='[[5g2e]], [[Resolution|resolution]] 6.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5g2e]] is a 24 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G2E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5G2E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5g2e]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G2E FirstGlance]. <br> |
| - | </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=5g2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g2e OCA], [http://pdbe.org/5g2e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g2e RCSB], [http://www.ebi.ac.uk/pdbsum/5g2e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g2e ProSAT]</span></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]] 6.7Å</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=5g2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g2e OCA], [https://pdbe.org/5g2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g2e RCSB], [https://www.ebi.ac.uk/pdbsum/5g2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g2e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NAP1_YEAST NAP1_YEAST]] Acidic protein, which assembles histones into an octamer (in vitro). Involved in the regulation of the localization and the function of the septins during mitosis. Involved in the function of B-type cyclins.<ref>PMID:2016313</ref> <ref>PMID:7622566</ref> <ref>PMID:12058072</ref> <ref>PMID:18086883</ref> [[http://www.uniprot.org/uniprot/H2B11_XENLA H2B11_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/H2A1_XENLA H2A1_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/NAP1_YEAST NAP1_YEAST] Acidic protein, which assembles histones into an octamer (in vitro). Involved in the regulation of the localization and the function of the septins during mitosis. Involved in the function of B-type cyclins.<ref>PMID:2016313</ref> <ref>PMID:7622566</ref> <ref>PMID:12058072</ref> <ref>PMID:18086883</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 5g2e" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5g2e" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Histone 3D structures|Histone 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: AguilarGurrieri, C]] | + | [[Category: Large Structures]] |
| - | [[Category: Ebong, I O]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Larabi, A]] | + | [[Category: Xenopus laevis]] |
| - | [[Category: Panne, D]] | + | [[Category: AguilarGurrieri C]] |
| - | [[Category: Patel, N A]] | + | [[Category: Ebong IO]] |
| - | [[Category: Pugh, B F]] | + | [[Category: Larabi A]] |
| - | [[Category: Reja, R]] | + | [[Category: Panne D]] |
| - | [[Category: Robinson, C V]] | + | [[Category: Patel NA]] |
| - | [[Category: Schoehn, G]] | + | [[Category: Pugh BF]] |
| - | [[Category: Vinayachandran, V]] | + | [[Category: Reja R]] |
| - | [[Category: Yen, K]] | + | [[Category: Robinson CV]] |
| - | [[Category: Chromatin]] | + | [[Category: Schoehn G]] |
| - | [[Category: Dna binding protein]] | + | [[Category: Vinayachandran V]] |
| - | [[Category: H2a-h2b]] | + | [[Category: Yen K]] |
| - | [[Category: Histone]]
| + | |
| - | [[Category: Nucleosome assembly]]
| + | |
| - | [[Category: Nucleosome assembly protein 1]]
| + | |
| Structural highlights
Function
NAP1_YEAST Acidic protein, which assembles histones into an octamer (in vitro). Involved in the regulation of the localization and the function of the septins during mitosis. Involved in the function of B-type cyclins.[1] [2] [3] [4]
Publication Abstract from PubMed
Nap1 is a histone chaperone involved in the nuclear import of H2A-H2B and nucleosome assembly. Here, we report the crystal structure of Nap1 bound to H2A-H2B together with in vitro and in vivo functional studies that elucidate the principles underlying Nap1-mediated H2A-H2B chaperoning and nucleosome assembly. A Nap1 dimer provides an acidic binding surface and asymmetrically engages a single H2A-H2B heterodimer. Oligomerization of the Nap1-H2A-H2B complex results in burial of surfaces required for deposition of H2A-H2B into nucleosomes. Chromatin immunoprecipitation-exonuclease (ChIP-exo) analysis shows that Nap1 is required for H2A-H2B deposition across the genome. Mutants that interfere with Nap1 oligomerization exhibit severe nucleosome assembly defects showing that oligomerization is essential for the chaperone function. These findings establish the molecular basis for Nap1-mediated H2A-H2B deposition and nucleosome assembly.
Structural evidence for Nap1-dependent H2A-H2B deposition and nucleosome assembly.,Aguilar-Gurrieri C, Larabi A, Vinayachandran V, Patel NA, Yen K, Reja R, Ebong IO, Schoehn G, Robinson CV, Pugh BF, Panne D EMBO J. 2016 Jul 1;35(13):1465-82. doi: 10.15252/embj.201694105. Epub 2016 May, 25. PMID:27225933[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ishimi Y, Kikuchi A. Identification and molecular cloning of yeast homolog of nucleosome assembly protein I which facilitates nucleosome assembly in vitro. J Biol Chem. 1991 Apr 15;266(11):7025-9. PMID:2016313
- ↑ Kellogg DR, Kikuchi A, Fujii-Nakata T, Turck CW, Murray AW. Members of the NAP/SET family of proteins interact specifically with B-type cyclins. J Cell Biol. 1995 Aug;130(3):661-73. PMID:7622566
- ↑ Mortensen EM, McDonald H, Yates J 3rd, Kellogg DR. Cell cycle-dependent assembly of a Gin4-septin complex. Mol Biol Cell. 2002 Jun;13(6):2091-105. PMID:12058072 doi:http://dx.doi.org/10.1091/mbc.01-10-0500
- ↑ Calvert ME, Keck KM, Ptak C, Shabanowitz J, Hunt DF, Pemberton LF. Phosphorylation by casein kinase 2 regulates Nap1 localization and function. Mol Cell Biol. 2008 Feb;28(4):1313-25. Epub 2007 Dec 17. PMID:18086883 doi:http://dx.doi.org/MCB.01035-07
- ↑ Aguilar-Gurrieri C, Larabi A, Vinayachandran V, Patel NA, Yen K, Reja R, Ebong IO, Schoehn G, Robinson CV, Pugh BF, Panne D. Structural evidence for Nap1-dependent H2A-H2B deposition and nucleosome assembly. EMBO J. 2016 Jul 1;35(13):1465-82. doi: 10.15252/embj.201694105. Epub 2016 May, 25. PMID:27225933 doi:http://dx.doi.org/10.15252/embj.201694105
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