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==== | ==The cryo-EM structure of CENP-A nucleosome in complex with the phosphorylated CENP-C== | ||
<StructureSection load='7by0' size='340' side='right'caption='[[7by0]]' scene=''> | <StructureSection load='7by0' size='340' side='right'caption='[[7by0]], [[Resolution|resolution]] 4.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7by0]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus], [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct] and [https://en.wikipedia.org/wiki/Unidentified_cloning_vector Unidentified cloning vector]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BY0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BY0 FirstGlance]. <br> | ||
</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=7by0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7by0 OCA], [https://pdbe.org/7by0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7by0 RCSB], [https://www.ebi.ac.uk/pdbsum/7by0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7by0 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.5Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></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=7by0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7by0 OCA], [https://pdbe.org/7by0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7by0 RCSB], [https://www.ebi.ac.uk/pdbsum/7by0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7by0 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The CENP-A nucleosome is a key structure for kinetochore assembly. Once the CENP-A nucleosome is established in the centromere, additional proteins recognize the CENP-A nucleosome to form a kinetochore. CENP-C and CENP-N are CENP-A binding proteins. We previously demonstrated that vertebrate CENP-C binding to the CENP-A nucleosome is regulated by CDK1-mediated CENP-C phosphorylation. However, it is still unknown how the phosphorylation of CENP-C regulates its binding to CENP-A. It is also not completely understood how and whether CENP-C and CENP-N act together on the CENP-A nucleosome. Here, using cryo-electron microscopy (cryo-EM) in combination with biochemical approaches, we reveal a stable CENP-A nucleosome-binding mode of CENP-C through unique regions. The chicken CENP-C structure bound to the CENP-A nucleosome is stabilized by an intramolecular link through the phosphorylated CENP-C residue. The stable CENP-A-CENP-C complex excludes CENP-N from the CENP-A nucleosome. These findings provide mechanistic insights into the dynamic kinetochore assembly regulated by CDK1-mediated CENP-C phosphorylation. | |||
Cryo-EM structure of the CENP-A nucleosome in complex with phosphorylated CENP-C.,Ariyoshi M, Makino F, Watanabe R, Nakagawa R, Kato T, Namba K, Arimura Y, Fujita R, Kurumizaka H, Okumura EI, Hara M, Fukagawa T EMBO J. 2021 Mar 1;40(5):e105671. doi: 10.15252/embj.2020105671. Epub 2021 Jan , 19. PMID:33463726<ref>PMID:33463726</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7by0" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Centromere protein 3D structure|Centromere protein 3D structure]] | |||
*[[Histone 3D structures|Histone 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Gallus gallus]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: Unidentified cloning vector]] | |||
[[Category: Ariyoshi M]] | |||
[[Category: Fukagawa T]] | |||
[[Category: Makino F]] | |||
Latest revision as of 11:37, 17 October 2024
The cryo-EM structure of CENP-A nucleosome in complex with the phosphorylated CENP-CThe cryo-EM structure of CENP-A nucleosome in complex with the phosphorylated CENP-C
Structural highlights
Publication Abstract from PubMedThe CENP-A nucleosome is a key structure for kinetochore assembly. Once the CENP-A nucleosome is established in the centromere, additional proteins recognize the CENP-A nucleosome to form a kinetochore. CENP-C and CENP-N are CENP-A binding proteins. We previously demonstrated that vertebrate CENP-C binding to the CENP-A nucleosome is regulated by CDK1-mediated CENP-C phosphorylation. However, it is still unknown how the phosphorylation of CENP-C regulates its binding to CENP-A. It is also not completely understood how and whether CENP-C and CENP-N act together on the CENP-A nucleosome. Here, using cryo-electron microscopy (cryo-EM) in combination with biochemical approaches, we reveal a stable CENP-A nucleosome-binding mode of CENP-C through unique regions. The chicken CENP-C structure bound to the CENP-A nucleosome is stabilized by an intramolecular link through the phosphorylated CENP-C residue. The stable CENP-A-CENP-C complex excludes CENP-N from the CENP-A nucleosome. These findings provide mechanistic insights into the dynamic kinetochore assembly regulated by CDK1-mediated CENP-C phosphorylation. Cryo-EM structure of the CENP-A nucleosome in complex with phosphorylated CENP-C.,Ariyoshi M, Makino F, Watanabe R, Nakagawa R, Kato T, Namba K, Arimura Y, Fujita R, Kurumizaka H, Okumura EI, Hara M, Fukagawa T EMBO J. 2021 Mar 1;40(5):e105671. doi: 10.15252/embj.2020105671. Epub 2021 Jan , 19. PMID:33463726[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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