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

A conserved mechanism for centromeric nucleosome recognition by centromere protein CENP-C.
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DOI:
10.1126/science.1235532
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发表时间:
2013-05-31
期刊:
Science (New York, N.Y.)
影响因子:
--
通讯作者:
Bai Y
Bai Y
中科院分区:
其他
文献类型:
--
作者:
Kato H;Jiang J;Zhou BR;Rozendaal M;Feng H;Ghirlando R;Xiao TS;Straight AF;Bai Y

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有丝分裂过程中的染色体分离需要在着丝粒上组装着丝粒复合体。着丝粒蛋白C(CENP-C)对着丝粒核小体中组蛋白变异体CENP-A的特异性识别是着丝粒组装的关键。我们定义了这种识别机制的决定因素,并发现CENP-C与CENP-A尾部的疏水区结合,并对接在组蛋白H_2A/H_2B的酸性斑块上。我们进一步发现,更广泛保守的CENP-C基序对CENP-A核小体识别使用了相同的机制。我们的发现揭示了蛋白质募集到着丝粒的保守机制和组蛋白识别模式,在组蛋白识别模式中,无序的肽通过核小体对接促进的疏水作用与组蛋白尾部结合。
Chromosome segregation during mitosis requires assembly of the kinetochore complex at the centromere. Key to kinetochore assembly is the 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/H2B. We further find 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 nucleosome-docking-facilitated hydrophobic interactions.
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