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| | <StructureSection load='5jbm' size='340' side='right'caption='[[5jbm]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='5jbm' size='340' side='right'caption='[[5jbm]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jbm]] is a 1 chain structure with sequence from [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=5JBM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JBM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jbm]] is a 1 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=5JBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JBM FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RLF2, CAC1, YPR018W, YP9531.12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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]] 3Å</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=5jbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jbm OCA], [http://pdbe.org/5jbm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jbm RCSB], [http://www.ebi.ac.uk/pdbsum/5jbm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jbm 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=5jbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jbm OCA], [https://pdbe.org/5jbm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jbm RCSB], [https://www.ebi.ac.uk/pdbsum/5jbm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jbm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RLF2_YEAST RLF2_YEAST]] Acts as a component of chromatin assembly factor 1 (CAF-1), which assembles histone octamers onto replicating DNA in vitro. It performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. p90 may facilitate the efficient and timely assembly of histones into telomeric chromatin. | + | [https://www.uniprot.org/uniprot/RLF2_YEAST RLF2_YEAST] Acts as a component of chromatin assembly factor 1 (CAF-1), which assembles histone octamers onto replicating DNA in vitro. It performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. p90 may facilitate the efficient and timely assembly of histones into telomeric chromatin. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Churchill, M E.A]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Liu, W]] | + | [[Category: Churchill MEA]] |
| - | [[Category: Zhou, Y]] | + | [[Category: Liu W]] |
| - | [[Category: Caf-1]] | + | [[Category: Zhou Y]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Histone chaperone]]
| + | |
| - | [[Category: Nucleosome assembly]]
| + | |
| Structural highlights
Function
RLF2_YEAST Acts as a component of chromatin assembly factor 1 (CAF-1), which assembles histone octamers onto replicating DNA in vitro. It performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. p90 may facilitate the efficient and timely assembly of histones into telomeric chromatin.
Publication Abstract from PubMed
The histone chaperone Chromatin Assembly Factor 1 (CAF-1) deposits tetrameric (H3/H4)2 histones onto newly-synthesized DNA during DNA replication. To understand the mechanism of the tri-subunit CAF-1 complex in this process, we investigated the protein-protein interactions within the CAF-1-H3/H4 architecture using biophysical and biochemical approaches. Hydrogen/deuterium exchange and chemical cross-linking coupled to mass spectrometry reveal interactions that are essential for CAF-1 function in budding yeast, and importantly indicate that the Cac1 subunit functions as a scaffold within the CAF-1-H3/H4 complex. Cac1 alone not only binds H3/H4 with high affinity, but also promotes histone tetramerization independent of the other subunits. Moreover, we identify a minimal region in the C-terminus of Cac1, including the structured winged helix domain and glutamate/aspartate-rich domain, which is sufficient to induce (H3/H4)2 tetramerization. These findings reveal a key role of Cac1 in histone tetramerization, providing a new model for CAF-1-H3/H4 architecture and function during eukaryotic replication.
The Cac1 subunit of histone chaperone CAF-1 organizes CAF-1-H3/H4 architecture and tetramerizes histones.,Liu WH, Roemer SC, Zhou Y, Shen ZJ, Dennehey BK, Balsbaugh JL, Liddle JC, Nemkov T, Ahn NG, Hansen KC, Tyler JK, Churchill ME Elife. 2016 Sep 30;5. pii: e18023. doi: 10.7554/eLife.18023. PMID:27690308[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu WH, Roemer SC, Zhou Y, Shen ZJ, Dennehey BK, Balsbaugh JL, Liddle JC, Nemkov T, Ahn NG, Hansen KC, Tyler JK, Churchill ME. The Cac1 subunit of histone chaperone CAF-1 organizes CAF-1-H3/H4 architecture and tetramerizes histones. Elife. 2016 Sep 30;5. pii: e18023. doi: 10.7554/eLife.18023. PMID:27690308 doi:http://dx.doi.org/10.7554/eLife.18023
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