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Visualized heterooligomeric subunit structures of 817 human cellular proteins by correlating native protein 2D maps with protein interaction databases
Journal of Chromatography B ( IF 3 ) Pub Date : 2020-12-21 , DOI: 10.1016/j.jchromb.2020.122509
Ya Jin , Takashi Manabe

Previously, we have reported on the reconstruction of 4323 native protein 2D maps of human bronchial smooth muscle cells (HBSMC) by combining nondenaturing 2DE, grid gel-cutting, and quantitative LC-MS/MS. In this work, we report on the visualization of the heterooligomeric subunit structures of HBSMC proteins by correlating the native protein 2D maps with the information in protein interaction databases. Image analysis of the 2D maps was employed as the first approach. Each of the native protein 2D maps of 2327 proteins, which had three or more detected squares in the native protein 2D maps, was compared with the 2D maps of the remaining 2326 proteins scoring the degree of overlap in an area around the quantity peak and the protein partner which showed the best score was decided. The protein pairs were examined on their reported interactions referring to protein interaction databases. In order to consider the cases where a protein has multiple functions and the heterooligomeric subunit structures might not be detected from the image analysis, prior database search was employed as the second approach. Each of the 1689 HBSMC proteins, which had five or more detected squares in the native protein 2D maps, was examined on its interactor proteins described in the databases, then the native 2D map was compared with the maps of the interactor proteins to find the overlap which reasonably supported the interaction. Summarizing these examinations, 215 heterooligomeric subunit structures of 817 human cellular proteins could be visualized on the native protein 2D maps.



中文翻译:

通过将天然蛋白质2D图与蛋白质相互作用数据库相关联,可视化817个人类细胞蛋白质的杂聚寡聚亚基结构

以前,我们已经报道了结合非变性2DE,网格凝胶切割和定量LC-MS / MS重建人支气管平滑肌细胞(HBSMC)的4323个天然蛋白质2D图的方法。在这项工作中,我们通过将天然蛋白质2D图谱与蛋白质相互作用数据库中的信息相关联,报告了HBSMC蛋白质的异寡聚亚基结构的可视化。二维地图的图像分析被用作第一种方法。将2327个蛋白质的每个天然蛋白质2D图(在该天然蛋白质2D图中具有三个或更多检测到的正方形)与其余2326个蛋白质的2D图(在数量峰和区域周围的重叠程度得分)进行了比较。确定表现最佳的蛋白质伴侣。参照蛋白质相互作用数据库检查蛋白质对的报告相互作用。为了考虑蛋白质具有多种功能并且可能无法从图像分析中检测到异源寡聚亚基结构的情况,将先前的数据库搜索用作第二种方法。在数据库中描述的其相互作用蛋白上检查了在天然蛋白2D图中具有五个或更多检测到的正方形的1689种HBSMC蛋白质中的每一个,然后将天然2D图与该相互作用蛋白的图进行比较以发现重叠合理地支持了互动。总结这些检查,可以在天然蛋白质2D图上可视化817个人类细胞蛋白质的215个异源寡聚亚基结构。为了考虑蛋白质具有多种功能并且可能无法从图像分析中检测到异源寡聚亚基结构的情况,将先前的数据库搜索用作第二种方法。在数据库中描述的其相互作用蛋白上检查了在天然蛋白2D图中具有五个或更多检测到的正方形的1689种HBSMC蛋白质中的每一个,然后将天然2D图与该相互作用蛋白的图进行比较以发现重叠合理地支持了互动。总结这些检查,可以在天然蛋白质2D图上可视化817个人类细胞蛋白质的215个异源寡聚亚基结构。为了考虑蛋白质具有多种功能并且可能无法从图像分析中检测到异源寡聚亚基结构的情况,将先前的数据库搜索用作第二种方法。在数据库中描述的其相互作用蛋白上检查了在天然蛋白2D图中具有五个或更多检测到的正方形的1689种HBSMC蛋白质中的每一个,然后将天然2D图与该相互作用蛋白的图进行比较以发现重叠合理地支持了互动。总结这些检查,可以在天然蛋白质2D图上可视化817个人类细胞蛋白质的215个异源寡聚亚基结构。先前的数据库搜索被用作第二种方法。在数据库中描述的其相互作用蛋白上检查了在天然蛋白2D图中具有五个或更多检测到的正方形的1689种HBSMC蛋白质中的每一个,然后将天然2D图与该相互作用蛋白的图进行比较以发现重叠合理地支持了互动。总结这些检查,可以在天然蛋白质2D图上可视化817个人类细胞蛋白质的215个异源寡聚亚基结构。先前的数据库搜索被用作第二种方法。在数据库中描述的其相互作用蛋白上检查了在天然蛋白2D图中具有五个或更多检测到的正方形的1689种HBSMC蛋白质中的每一个,然后将天然2D图与该相互作用蛋白的图进行比较以发现重叠合理地支持了互动。总结这些检查,可以在天然蛋白质2D图上可视化817个人类细胞蛋白质的215个异源寡聚亚基结构。

更新日期:2021-01-05
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