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首页> 美国卫生研究院文献>The Journal of Biological Chemistry >Complementary Interhelical Interactions between Three Buried Glu-Lys Pairs within Three Heptad Repeats Are Essential for Hec1-Nuf2 Heterodimerization and Mitotic Progression
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Complementary Interhelical Interactions between Three Buried Glu-Lys Pairs within Three Heptad Repeats Are Essential for Hec1-Nuf2 Heterodimerization and Mitotic Progression

机译：三个Heptad重复中的三个埋入的Glu-Lys对之间的互补螺旋间相互作用对于Hec1-Nuf2异二聚化和有丝分裂进程至关重要。

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Hec1 and Nuf2, core components of the NDC80 complex, are essential for kinetochore-microtubule attachment and chromosome segregation. It has been shown that both Hec1 and Nuf2 utilize their coiled-coil domains to form a functional dimer; however, details of the consequential significance and structural requirements to form the dimerization interface have yet to be elucidated. Here, we showed that Hec1 required three contiguous heptad repeats from Leu-324 to Leu-352, but not the entire first coiled-coil domain, to ensure overall stability of the NDC80 complex through direct interaction with Nuf2. Substituting the hydrophobic core residues, Leu-331, Val-338, and Ile-345, of Hec1 with alanine completely eliminated Nuf2 binding and blocked mitotic progression. Moreover, unlike most coiled-coil proteins, where the buried positions are composed of hydrophobic residues, Hec1 possessed an unusual distribution of glutamic acid residues, Glu-334, Glu-341, and Glu-348, buried within the interior dimerization interface, which complement with three Nuf2 lysine residues: Lys-227, Lys-234, and Lys-241. Substituting these corresponding residues with alanine diminished the binding affinity between Hec1 and Nuf2, compromised NDC80 complex formation, and adversely affected mitotic progression. Taken together, these findings demonstrated that three buried glutamic acid-lysine pairs, in concert with hydrophobic interactions of core residues, provide the major specificity and stability requirements for Hec1-Nuf2 dimerization and NDC80 complex formation.
机译：Hec1和Nuf2是NDC80复合体的核心组成部分，对于线粒体-微管附着和染色体分离至关重要。已经表明，Hec1和Nuf2都利用它们的卷曲螺旋结构域来形成功能性二聚体。然而，关于形成二聚界面的重要性和结构要求的细节尚未阐明。在这里，我们表明，Hec1需要从Leu-324到Leu-352的三个连续的七肽重复序列，而不是整个第一个螺旋线圈域，以确保通过与Nuf2的直接相互作用来确保NDC80复合物的整体稳定性。用丙氨酸代替Hec1的疏水核心残基Leu-331，Val-338和Ile-345，可以完全消除Nuf2结合并阻断有丝分裂进程。此外，与大多数卷曲螺旋蛋白不同，其埋藏位置由疏水残基组成，Hec1具有不寻常的谷氨酸残基分布，Glu-334，Glu-341和Glu-348埋在内部二聚化界面中，与三个Nuf2赖氨酸残基互补：Lys-227，Lys-234和Lys-241。用丙氨酸取代这些相应的残基会减少Hec1和Nuf2之间的结合亲和力，损害NDC80复合物的形成，并不利地影响有丝分裂进程。综上所述，这些发现表明，三个掩埋的谷氨酸-赖氨酸对与核心残基的疏水相互作用协同作用，为Hec1-Nuf2二聚化和NDC80复合物的形成提供了主要的特异性和稳定性要求。

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