人类着丝粒蛋白A包含一个与组蛋白H3相关的组蛋白折叠结构域，该结构域是靶向着丝粒所必需的。
Human CENP-A contains a histone H3 related histone fold domain that is required for targeting to the centromere.
作者信息
Sullivan K F, Hechenberger M, Masri K
机构信息
Department of Cell Biology, Scripps Research Institute, La Jolla, California 92037.
出版信息
J Cell Biol. 1994 Nov;127(3):581-92. doi: 10.1083/jcb.127.3.581.
Abstract
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.
摘要
着丝粒是决定染色体有丝分裂行为的特殊染色体结构域。为了研究着丝粒染色质特异性的分子基础，我们克隆了一个编码17kD组蛋白样着丝粒抗原CENP-A的人类cDNA。在140个氨基酸的CENP-A多肽中可明显看出两个结构域：一个独特的NH2末端结构域和一个与核小体核心蛋白组蛋白H3有62%同源性的93个氨基酸的COOH末端结构域。当在多种动物细胞中表达时，CENP-A的一个表位标记衍生物能准确地定位于着丝粒，并且这种定位活性存在于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一种新型核心组蛋白掺入着丝粒染色质所驱动的。
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