Subunit interactions and arrangements in the fission yeast Mis16–Mis18–Mis19 complex

Centromeric chromatin in fission yeast is distinguished by the presence of nucleosomes containing the histone H3 variant Cnp1(CENP-A). Cell cycle–specific deposition of Cnp1 requires the Mis16–Mis18–Mis19 complex, which is thought to direct recruitment of Scm3-chaperoned Cnp1/histone H4 dimers to DN...

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Autores principales: Korntner-Vetter, Melanie, Lefèvre, Stéphane, Hu, Xiao-Wen, George, Roger, Singleton, Martin R
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Life Science Alliance LLC 2019
Materias:
Research Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6677171/
https://www.ncbi.nlm.nih.gov/pubmed/31371524
http://dx.doi.org/10.26508/lsa.201900408
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author Korntner-Vetter, Melanie
Lefèvre, Stéphane
Hu, Xiao-Wen
George, Roger
Singleton, Martin R
author_facet Korntner-Vetter, Melanie
Lefèvre, Stéphane
Hu, Xiao-Wen
George, Roger
Singleton, Martin R
author_sort Korntner-Vetter, Melanie
collection PubMed
description Centromeric chromatin in fission yeast is distinguished by the presence of nucleosomes containing the histone H3 variant Cnp1(CENP-A). Cell cycle–specific deposition of Cnp1 requires the Mis16–Mis18–Mis19 complex, which is thought to direct recruitment of Scm3-chaperoned Cnp1/histone H4 dimers to DNA. Here, we present the structure of the essential Mis18 partner protein Mis19 and describe its interaction with Mis16, revealing a bipartite-binding site. We provide data on the stoichiometry and overall architecture of the complex and provide detailed insights into the Mis18–Mis19 interface.
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spelling pubmed-66771712019-08-07 Subunit interactions and arrangements in the fission yeast Mis16–Mis18–Mis19 complex Korntner-Vetter, Melanie Lefèvre, Stéphane Hu, Xiao-Wen George, Roger Singleton, Martin R Life Sci Alliance Research Articles Centromeric chromatin in fission yeast is distinguished by the presence of nucleosomes containing the histone H3 variant Cnp1(CENP-A). Cell cycle–specific deposition of Cnp1 requires the Mis16–Mis18–Mis19 complex, which is thought to direct recruitment of Scm3-chaperoned Cnp1/histone H4 dimers to DNA. Here, we present the structure of the essential Mis18 partner protein Mis19 and describe its interaction with Mis16, revealing a bipartite-binding site. We provide data on the stoichiometry and overall architecture of the complex and provide detailed insights into the Mis18–Mis19 interface. Life Science Alliance LLC 2019-08-01 /pmc/articles/PMC6677171/ /pubmed/31371524 http://dx.doi.org/10.26508/lsa.201900408 Text en © 2019 Korntner-Vetter et al. https://creativecommons.org/licenses/by/4.0/This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/licenses/by/4.0/).
spellingShingle Research Articles
Korntner-Vetter, Melanie
Lefèvre, Stéphane
Hu, Xiao-Wen
George, Roger
Singleton, Martin R
Subunit interactions and arrangements in the fission yeast Mis16–Mis18–Mis19 complex
title Subunit interactions and arrangements in the fission yeast Mis16–Mis18–Mis19 complex
title_full Subunit interactions and arrangements in the fission yeast Mis16–Mis18–Mis19 complex
title_fullStr Subunit interactions and arrangements in the fission yeast Mis16–Mis18–Mis19 complex
title_full_unstemmed Subunit interactions and arrangements in the fission yeast Mis16–Mis18–Mis19 complex
title_short Subunit interactions and arrangements in the fission yeast Mis16–Mis18–Mis19 complex
title_sort subunit interactions and arrangements in the fission yeast mis16–mis18–mis19 complex
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6677171/
https://www.ncbi.nlm.nih.gov/pubmed/31371524
http://dx.doi.org/10.26508/lsa.201900408
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