Mis16 Switches Function from a Histone H4 Chaperone to a CENP-A^Cnp1-Specific Assembly Factor through Eic1 Interaction.

ABSTRACT: 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 t

SUBMITTER: An S 

PROVIDER: S-EPMC6031460 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature