6s1r
Structure of fission yeast Mis16 bound to histone H4
Structural highlights
FunctionHAT2_SCHPO Regulatory subunit of the histone acetylase B (HAT-B) complex (By similarity). The complex acetylates 'Lys-12' of histone H4 which is required for telomeric silencing (By similarity). Component of the CENP-A recruiting complex that ensures the integrity of mitotic spindles through maintenance of kinetochore factors mis6/CENP-I and cnp1/CENP-A (PubMed:15369671, PubMed:24774534, PubMed:24789708, PubMed:25375240). Maintains the deacetylated state of histones specifically in the central core of the centromeres (PubMed:15369671).[UniProtKB:P39984][1] [2] [3] [4] Publication Abstract from PubMedCentromeric 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. Subunit interactions and arrangements in the fission yeast Mis16-Mis18-Mis19 complex.,Korntner-Vetter M, Lefevre S, Hu XW, George R, Singleton MR Life Sci Alliance. 2019 Aug 1;2(4). pii: 2/4/e201900408. doi:, 10.26508/lsa.201900408. Print 2019 Aug. PMID:31371524[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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