5wjc

Crystal structure of Schizosaccharomyces pombe Mis16 in complex with Eic1

spinqualitylabelsall models 5wjc, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5wjc is a 2 chain structure with sequence from Fission yeast. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: mis16, hat2, SPCC1672.10 (Fission yeast), SPBC27B12.02, SPBC30B4.10 (Fission yeast) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [HAT2_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] [MIS19_SCHPO] 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:24774534, PubMed:24789708, PubMed:25375240). Links mis16 and mis18 to recruit CENP-A through interacting with non-sense-mediated mRNA decay (NMD) factors and the SWI/SNF complex (PubMed:24774534). Links also mis18 with the CCAN/mis6/ctf19 complex to promote CENP-A assembly (PubMed:24789708). Publication Abstract from PubMed The Mis18 complex, composed of Mis16, Eic1, and Mis18 in fission yeast, selectively deposits the centromere-specific histone H3 variant, CENP-A(Cnp1), at centromeres. How the intact Mis18 holo-complex oligomerizes and how Mis16, a well-known ubiquitous histone H4 chaperone, plays a centromere-specific role in the Mis18 holo-complex, remain unclear. Here, we report the stoichiometry of the intact Mis18 holo-complex as (Mis16)2:(Eic1)2:(Mis18)4 using analytical ultracentrifugation. We further determine the crystal structure of Schizosaccharomyces pombe Mis16 in complex with the C-terminal portion of Eic1 (Eic1-CT). Notably, Mis16 accommodates Eic1-CT through the binding pocket normally occupied by histone H4, indicating that Eic1 and H4 compete for the same binding site, providing a mechanism for Mis16 to switch its binding partner from histone H4 to Eic1. Thus, our analyses not only determine the stoichiometry of the intact Mis18 holo-complex but also uncover the molecular mechanism by which Mis16 plays a centromere-specific role through Eic1 association. Mis16 Switches Function from a Histone H4 Chaperone to a CENP-A(Cnp1)-Specific Assembly Factor through Eic1 Interaction.,An S, Koldewey P, Chik J, Subramanian L, Cho US Structure. 2018 May 1. pii: S0969-2126(18)30137-0. doi:, 10.1016/j.str.2018.04.012. PMID:29804820 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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