The centromeric chromatin plays an essential role in regulating the attachment of microtubules and controlling the segregation of sister chromatids during mitosis. In budding yeast, the evolutionary conserved histone variant, Cse4 is a vital component of the multiprotein kinetochore complex and is recruited to the centromere through its chaperone, Suppressor of chromosome mis-segregation (Scm3). Scm3 is an inner kinetochore protein crucial for the formation of a functional inner kinetochore. Scm3 has been known to play an active role in the assembly of the centromeric nucleosome and its deletion has been found to have deleterious effects on the cells leading to chromosome segregation defects. However, structural details of monomeric full length Scm3 have remained elusive so far. Here, we report the backbone and side-chain resonance assignments of centromeric protein, Scm3. ¹H, ¹³C and ¹⁵N chemical shifts of Scm3 have been obtained by various 2D and 3D heteronuclear NMR experiments at pH 7.4 and 283 K.

中文翻译：

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来自酿酒酵母的着丝粒蛋白Scm3的骨架和侧链共振分配。

着丝粒染色质在调节微管的附着和控制有丝分裂过程中姐妹染色单体的分离中起着至关重要的作用。在发芽的酵母中，它是进化保守的组蛋白变体，Cse4是多蛋白动线粒复合体的重要组成部分，并通过其伴侣（染色体错位抑制子）（Scm3）被募集到着丝粒中。Scm3是内部功能性蛋白质，对功能性内部功能性蛋白质的形成至关重要。已知Scm3在着丝粒核小体的组装中起积极作用，并且发现其缺失对导致染色体分离缺陷的细胞具有有害作用。但是，到目前为止，单体全长Scm3的结构细节仍然难以捉摸。这里，通过在pH 7.4和283 K下进行的各种2D和3D异核NMR实验，获得了Scm3的¹ H，¹³ C和¹⁵ N化学位移。