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

Life Sci Alliance. 2019 Aug 1;2(4):e201900408. doi: 10.26508/lsa.201900408. Print 2019 Aug.

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.

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