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首页> 外文期刊>Journal of Molecular Biology >The microtubule binding properties of CENP-E's C-terminus and CENP-F
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The microtubule binding properties of CENP-E's C-terminus and CENP-F

机译：CENP-E的C末端和CENP-F的微管结合特性

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摘要

CENP-E (centromere protein E) and CENP-F (centromere protein F), also known as mitosin, are large, multi-functional proteins associated with the outer kinetochore. CENP-E features a well-characterized kinesin motor domain at its N-terminus and a second microtubule-binding domain at its C-terminus of unknown function. CENP-F is important for the formation of proper kinetochore- microtubule attachment and, similar to CENP-E, contains two microtubule-binding domains at its termini. While the importance of these proteins is known, the details of their interactions with microtubules have not yet been investigated. We have biochemically and structurally characterized the microtubule-binding properties of the amino- and carboxyl-terminal domains of CENP-F as well as the carboxyl-terminal (non-kinesin) domain of CENP-E. CENP-E's C-terminus and CENP-F's N-terminus bind microtubules with similar affinity to the well-characterized Ndc80 complex, while CENP-F's C-terminus shows much lower affinity. Electron microscopy analysis reveals that all of these domains engage the microtubule surface in a disordered manner, suggesting that these factors have no favored binding geometry and may allow for initial side-on attachments early in mitosis.
机译：CENP-E（着丝粒蛋白E）和CENP-F（着丝粒蛋白F），也称为丝裂素，是与外部动粒相关的大型多功能蛋白。 CENP-E在其N末端具有特征明确的驱动蛋白运动域，在其C末端具有未知功能的第二个微管结合域。 CENP-F对于形成适当的动线粒-微管附着很重要，并且与CENP-E相似，其末端含有两个微管结合域。尽管这些蛋白质的重要​​性是已知的，但尚未研究它们与微管相互作用的细节。我们已经生化和结构上表征了CENP-F的氨基和羧基末端结构域以及CENP-E的羧基末端（非驱动蛋白）结构域的微管结合特性。 CENP-E的C末端和CENP-F的N末端与微管的结合与特征明确的Ndc80复合物具有相似的亲和力，而CENP-F的C末端显示的亲和力低得多。电子显微镜分析表明，所有这些结构域均以无序的方式与微管表面结合，表明这些因素没有有利的结合几何结构，并且可能在有丝分裂的早期允许最初的侧面附着。

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