Human CENP-A contains a histone H3 related histone fold domain that is required for targeting to the centromere.
Human CENP-A contains a histone H3 related histone fold domain that is required for targeting to the centromere.
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DOI：
10.1083/jcb.127.3.581
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发表时间：
1994-11
期刊：
影响因子：
--
通讯作者：
Masri K
中科院分区：
文献类型：
--
作者：
Sullivan KF;Hechenberger M;Masri K
着丝粒是指定染色体有丝分裂行为的分化染色体结构域。为了检查着丝粒染色质规范的分子基础，我们克隆了编码 17-kD 组蛋白样着丝粒抗原 CENP-A 的人类 cDNA。 140 个氨基酸的 CENP-A 多肽中有两个明显的结构域：一个独特的 NH2 末端结构域和一个 93 个氨基酸的 COOH 末端结构域，与核小体核心蛋白组蛋白 H3 具有 62% 的同一性。当在多种动物细胞中表达时，CENP-A 的表位标记衍生物忠实地靶向着丝粒，并且这种靶向活性被证明存在于 CENP-A 的组蛋白样 COOH 末端结构域中。这些数据清楚地表明着丝粒的组装至少部分是由新型核心组蛋白掺入着丝粒染色质驱动的。
Centromeres are the differentiated chromosomal domains that specify the mitotic behavior of chromosomes. To examine the molecular basis for the specification of centromeric chromatin, we have cloned a human cDNA that encodes the 17-kD histone-like centromere antigen, CENP-A. Two domains are evident in the 140 aa CENP-A polypeptide: a unique NH2- terminal domain and a 93-amino acid COOH-terminal domain that shares 62% identity with nucleosomal core protein, histone H3. An epitope tagged derivative of CENP-A was faithfully targeted to centromeres when expressed in a variety of animal cells and this targeting activity was shown to reside in the histone-like COOH-terminal domain of CENP-A. These data clearly indicate that the assembly of centromeres is driven, at least in part, by the incorporation of a novel core histone into centromeric chromatin.