Human CENP-A contains a histone H3 related histone fold domain that is required for targeting to the centromere.

作者：Kevin F. Sullivan, Mirko Hechenberger, KA Masri · 发表于：The Journal of Cell Biology · 年份：1994 · DOI：10.1083/jcb.127.3.581 · 被引用次数：474 · 研究领域：Chromosomal and Genetic Variations、Genomics and Chromatin Dynamics、Microtubule and mitosis dynamics

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.