组蛋白伴侣中存在一个常见的结构主题，它模拟了组蛋白间的接触。
A common structural theme in histone chaperones mimics interhistone contacts.
机构信息
MRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, UK.
出版信息
Trends Biochem Sci. 2013 Jul;38(7):333-6. doi: 10.1016/j.tibs.2013.04.002.
Histones are among the most conserved proteins in eukaryotes: the structural constraints of the nucleosome pose a challenge to evolving novel function. Nevertheless, confined histone surfaces have diversified, allowing the modulation of basic chromatin function through specialized histone chaperones. Recent structures of three histone-chaperone complexes, DAXX, HJURP, and Scm3, exemplify a common parsimonious solution to the restricted evolutionary space of histone recognition by their cognate histone chaperones: the reutilization of existing themes in histone structural biology.
组蛋白是真核生物中最保守的蛋白质之一
核小体的结构限制对进化新功能构成了挑战。然而，受限制的组蛋白表面已经多样化，使得通过专门的组蛋白伴侣来调节基本染色质功能成为可能。最近的三个组蛋白伴侣复合物（DAXX、HJURP 和 Scm3）的结构，体现了其同源组蛋白伴侣在有限的组蛋白识别进化空间中一个共同的简约解决方案：在组蛋白结构生物学中重新利用现有的主题。
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