Extended Data Fig. 7: The S. cerevisiae Cenp-ANuc nucleosome is unwrapped.
From: Structure of the inner kinetochore CCAN complex assembled onto a centromeric nucleosome
a–c, The positively charged electrostatic potential of the DNA-binding groove of Cenp-LN subcomplex is conserved in S. cerevisiae, S. pombe and H. sapiens. S. pombe and H. sapiens are represented by modelled structures. d, Cenp-N interacts with S. cerevisiae Cenp-ANuc in the context of CCAN differently from the interaction of free human Cenp-N with Cenp-ANuc. The Cenp-N subunit of the human Cenp-N–Cenp-A nucleosome structure (PDB: 6C0W29) was superimposed onto Cenp-N of the S. cerevisiae CCAN–Cenp-ANuc structure. In this mode of Cenp-N–Cenp-ANuc interactions, Cenp-ANuc would clash with Cenp-OPQU+ and Cenp-N of CCAN. e, f, Structures of S. cerevisiae H3Nuc (PDB: 1ID324) (e) and Cenp-ANuc (f, this work). g, Sequence alignment of the N-terminal regions of S. cerevisiae H3 and Cenp-A (Cse4) histones. For the chimeric H3N–Cenp-ANuc, residues 1–50 of S. cerevisiae H3 were substituted for residues 1–140 of S. cerevisiae Cenp-A. A similar approach was used for vertebrate Cenp-ANuc (ref. 23).
