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

ABSTRACT: Human 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 human CENP-C central region (CENP-CCR), the main CENP-A binding module of CENP-C. We establish that the short ?N-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-CCR and CENP-Cmotif) both bind exclusively to the CENP-A nucleosome. We find CENP-CCR to bind with high affinity due to an extended hydrophobi

SUBMITTER: Dr. Nikolina Sekulic 

PROVIDER: S-SCDT-EMBOR-2019-48913V1 | biostudies-other |

REPOSITORIES: biostudies-other