5WJC

Crystal structure of Schizosaccharomyces pombe Mis16 in complex with Eic1

Summary for 5WJC

• Entry DOI: 10.2210/pdb5wjc/pdb
• Descriptor: Kinetochore protein Mis16, Eic1 protein (3 entities in total)
• Functional Keywords: fission yeast chaperone for histone h4, subcomponent of mis18 complex, eic1 binding, wd-40 repeats domain, protein binding
• Biological source: Schizosaccharomyces pombe 972h- (Fission yeast); More
• Total number of polymer chains: 2
• Total formula weight: 61935.30

Authors

An, S.,Cho, U.-S.,Koldewey, P.,Chik, J.,Subramanian, L. (deposition date: 2017-07-21, release date: 2018-06-27, Last modification date: 2023-10-04)

Primary citation

An, S.,Koldewey, P.,Chik, J.,Subramanian, L.,Cho, U.S.
Mis16 Switches Function from a Histone H4 Chaperone to a CENP-ACnp1-Specific Assembly Factor through Eic1 Interaction.
Structure, 26:960-, 2018

PubMed Abstract: The Mis18 complex, composed of Mis16, Eic1, and Mis18 in fission yeast, selectively deposits the centromere-specific histone H3 variant, CENP-A, 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):(Eic1):(Mis18) 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.

PubMed: 29804820
DOI: 10.1016/j.str.2018.04.012

Experimental method

X-RAY DIFFRACTION (2.298 Å)