CENP-C unwraps the human CENP-A nucleosome through the H2A C-terminal tail.

ABSTRACT: Centromeres are defined epigenetically by nucleosomes containing the histone H3 variant CENP-A, upon which the constitutive centromere-associated network of proteins (CCAN) is built. CENP-C is considered to be a central organizer of the CCAN. We provide new molecular insights into the structure of human CENP-A nucleosomes, in isolation and in complex with the CENP-C central region (CENP-C^CR ), the main CENP-A binding module of human CENP-C. We establish that the short αN helix of CENP-A promotes DNA flexibility at the nucleosome ends, independently of the sequence it wraps. Furthermore, we show that, in vitro, two regions of human CENP-C (CENP-C^CR and CENP-C^motif ) both bind exclusively to the CENP-A nucleosome. We find CENP-C^CR to bind with high

SUBMITTER: Ali-Ahmad A 

PROVIDER: S-EPMC6776904 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature