A conserved mechanism for centromeric nucleosome recognition by centromere protein CENP-C.

Kato, Hidenori; Jiang, Jiansheng; Zhou, Bing-Rui; Rozendaal, Marieke; Feng, Hanqiao; Ghirlando, Rodolfo; Xiao, T Sam; Straight, Aaron F et al. · Science · 2013

basic_science · Level V

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Abstract

Chromosome segregation during mitosis requires assembly of the kinetochore complex at the centromere. Kinetochore assembly depends on specific recognition of the histone variant CENP-A in the centromeric nucleosome by centromere protein C (CENP-C). We have defined the determinants of this recognition mechanism and discovered that CENP-C binds a hydrophobic region in the CENP-A tail and docks onto the acidic patch of histone H2A and H2B. We further found that the more broadly conserved CENP-C motif uses the same mechanism for CENP-A nucleosome recognition. Our findings reveal a conserved mechanism for protein recruitment to centromeres and a histone recognition mode whereby a disordered peptide binds the histone tail through hydrophobic interactions facilitated by nucleosome docking.

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