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Phosphorylation in the accessory domain of yeast histone chaperone protein 1 exposes the nuclear export signal sequence
Proteins: Structure, Function, and Bioinformatics ( IF 3.2 ) Pub Date : 2021-09-18 , DOI: 10.1002/prot.26240
Sho Ashida 1 , Rikuri Morita 2 , Yasuteru Shigeta 2 , Ryuhei Harada 2
Affiliation  

Histone chaperone proteins assist in the formation of the histone octamers, the scaffold proteins that facilitate the packing of DNA into nucleosomes in the cell nucleus. One such histone chaperone protein is yeast nucleosome assembly protein 1 (yNap1), the crystal structure of which has been determined and found to have a nuclear export signal (NES) sequence within its long α-helix. Experimental evidence obtained from mutagenesis studies of the budding yeast suggests that the NES is necessary for the transport of yNap1 from the cell nucleus to the cytosol. However, the NES sequence is masked by an accessory domain, the exact role of which has not yet been elucidated, especially in nucleocytoplasmic transport. To clarify the role of the accessory domain, we focused on its phosphorylation, because proteomic experiments have identified multiple phosphorylation sites on yNap1. To study this phenomenon computationally, all-atom molecular dynamics simulations of the non-phosphorylated yNap1 (Nap1-nonP) and phosphorylated yNap1 (Nap1-P) systems were performed. Specifically, we addressed how the NES sequence is exposed to the protein surface by measuring its solvent-accessible surface area (SASA). It was found that the median of the SASA distribution of Nap1-P was greater than that of Nap1-nonP, indicating that phosphorylation in the accessory domain exposes the NES, resulting in its increased accessibility. In conclusion, yNap1 might modulate the accessibility of the NES by dislocating the accessory domain through its phosphorylation.

中文翻译:

酵母组蛋白伴侣蛋白1辅助结构域的磷酸化暴露了核输出信号序列

组蛋白伴侣蛋白有助于组蛋白八聚体的形成,组蛋白八聚体是一种支架蛋白,可促进 DNA 包装到细胞核中的核小体中。一种这样的组蛋白伴侣蛋白是酵母核小体组装蛋白 1 (yNap1),其晶体结构已被确定并发现在其长 α-螺旋内具有核输出信号 (NES) 序列。从萌芽酵母的诱变研究中获得的实验证据表明,NES 是 yNap1 从细胞核转运到细胞质所必需的。然而,NES 序列被一个辅助结构域所掩盖,其确切作用尚未阐明,尤其是在核质转运中。为了阐明辅助结构域的作用,我们专注于它的磷酸化,因为蛋白质组学实验已经确定了 yNap1 上的多个磷酸化位点。为了通过计算研究这种现象,对非磷酸化 yNap1 (Nap1-nonP) 和磷酸化 yNap1 (Nap1-P) 系统进行了全原子分子动力学模拟。具体来说,我们通过测量其溶剂可及表面积 (SASA) 来解决 NES 序列如何暴露于蛋白质表面。发现 Nap1-P 的 SASA 分布的中位数大于 Nap1-nonP,表明辅助结构域中的磷酸化暴露了 NES,导致其可访问性增加。总之,yNap1 可能通过磷酸化使辅助结构域脱位来调节 NES 的可访问性。对非磷酸化 yNap1 (Nap1-nonP) 和磷酸化 yNap1 (Nap1-P) 系统进行了全原子分子动力学模拟。具体来说,我们通过测量其溶剂可及表面积 (SASA) 来解决 NES 序列如何暴露于蛋白质表面。发现 Nap1-P 的 SASA 分布的中位数大于 Nap1-nonP,表明辅助结构域中的磷酸化暴露了 NES,导致其可访问性增加。总之,yNap1 可能通过磷酸化使辅助结构域脱位来调节 NES 的可访问性。对非磷酸化 yNap1 (Nap1-nonP) 和磷酸化 yNap1 (Nap1-P) 系统进行了全原子分子动力学模拟。具体来说,我们通过测量其溶剂可及表面积 (SASA) 来解决 NES 序列如何暴露于蛋白质表面。发现 Nap1-P 的 SASA 分布的中位数大于 Nap1-nonP,表明辅助结构域中的磷酸化暴露了 NES,导致其可访问性增加。总之,yNap1 可能通过磷酸化使辅助结构域脱位来调节 NES 的可访问性。我们通过测量其溶剂可及表面积(SASA)来解决NES序列如何暴露于蛋白质表面。发现 Nap1-P 的 SASA 分布的中位数大于 Nap1-nonP,表明辅助结构域中的磷酸化暴露了 NES,导致其可访问性增加。总之,yNap1 可能通过磷酸化使辅助结构域脱位来调节 NES 的可访问性。我们通过测量其溶剂可及表面积(SASA)来解决NES序列如何暴露于蛋白质表面。发现 Nap1-P 的 SASA 分布的中位数大于 Nap1-nonP,表明辅助结构域中的磷酸化暴露了 NES,导致其可访问性增加。总之,yNap1 可能通过磷酸化使辅助结构域脱位来调节 NES 的可访问性。
更新日期:2021-09-18
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