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.
© 2019 Korntner-Vetter et al.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Binding Sites
-
Carrier Proteins / chemistry
-
Carrier Proteins / genetics
-
Carrier Proteins / metabolism*
-
Centromere / metabolism
-
Chromosomal Proteins, Non-Histone / metabolism
-
Histones / chemistry
-
Histones / metabolism
-
Models, Molecular
-
Multiprotein Complexes / chemistry
-
Multiprotein Complexes / genetics
-
Multiprotein Complexes / metabolism*
-
Mutation
-
Protein Binding
-
Schizosaccharomyces / genetics
-
Schizosaccharomyces / metabolism*
-
Schizosaccharomyces pombe Proteins / chemistry
-
Schizosaccharomyces pombe Proteins / genetics
-
Schizosaccharomyces pombe Proteins / metabolism*
Substances
-
Carrier Proteins
-
Chromosomal Proteins, Non-Histone
-
Cnp1 protein, S pombe
-
Histones
-
Mis16 protein, S pombe
-
Mis18 protein, S pombe
-
Mis19 protein, S pombe
-
Multiprotein Complexes
-
Schizosaccharomyces pombe Proteins
Associated data
-
PDB/4XYI
-
PDB/3CFS
-
PDB/5WAI
-
PDB/6S1L
-
PDB/6S1R
-
PDB/6S29