The centromere is epigenetically marked by a histone H3 variant-CENP-A. The budding yeast CENP-A called Cse4, consists of an unusually long N-terminus that is known to be involved in kinetochore assembly. Its disordered chaperone, Scm3 is responsible for the centromeric deposition of Cse4 as well as in the maintenance of a segregation-competent kinetochore. In this study, we show that the Cse4 N-terminus is intrinsically disordered and interacts with Scm3 at multiple sites, and the complex does not gain any substantial structure. Additionally, the complex forms a synergistic association with an essential inner kinetochore component (Ctf19-Mcm21-Okp1-Ame1), and a model has been suggested to this effect. Thus, our study provides mechanistic insights into the Cse4 N-terminus-chaperone interaction and also illustrates how intrinsically disordered proteins mediate assembly of complex multiprotein networks, in general.

中文翻译：

---

CENP-ACse4 尾部伴侣相互作用紊乱促进与 Ame1/Okp1 在动粒处的结合


着丝粒由组蛋白 H3 变体 -CENP-A 进行表观遗传学标记。芽殖酵母 CENP-A 称为 Cse4，由一个异常长的 N 末端组成，已知该末端参与着丝粒组装。其无序伴侣 Scm3 负责 Cse4 的着丝粒沉积以及维持具有分离能力的动粒。在这项研究中，我们发现 Cse4 N 末端本质上是无序的，并且在多个位点与 Scm3 相互作用，并且该复合物没有获得任何实质性结构。此外，该复合物与重要的内部动粒成分（Ctf19-Mcm21-Okp1-Ame1）形成协同关联，并且已经提出了一个模型来实现这种效果。因此，我们的研究提供了对 Cse4 N 末端-伴侣相互作用的机制见解，并且还说明了本质上无序的蛋白质如何介导复杂多蛋白网络的组装。