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

DOI: 10.26508/lsa.201900408 DOI Help

Authors: Melanie Korntner-vetter (The Francis Crick Institute) , Stéphane Lefèvre (The Francis Crick Institute) , Xiao-wen Hu (The Francis Crick Institute) , Roger George (The Francis Crick Institute (Midland Road)) , Martin R. Singleton (The Francis Crick Institute)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Life Science Alliance , VOL 2

State: Published (Approved)
Published: August 2019
Diamond Proposal Number(s): 9826

Open Access Open Access

Abstract: Centromeric chromatin in fission yeast is distinguished by the presence of nucleosomes containing the histone H3 variant Cnp1CENP-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.

Subject Areas: Biology and Bio-materials


Instruments: I04-Macromolecular Crystallography

Other Facilities: Swiss Light Source; ESRF

Documents:
e201900408.full.pdf