Systematically Ranking the Tightness of Membrane Association for Peripheral Membrane Proteins (PMPs)
Systematically Ranking the Tightness of Membrane Association for Peripheral Membrane Proteins (PMPs)
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DOI：
10.1074/mcp.m114.044800
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发表时间：
2015-02-01
影响因子：
7
通讯作者：
Wang, Yingchun
中科院分区：
文献类型：
--
作者：
Gao, Liyan;Ge, Haitao;Wang, Yingchun
大规模定量评价非跨膜蛋白的膜结合紧密性对于鉴定具有功能意义的真正外周膜蛋白是重要的。在此，我们同时排名超过1000个蛋白质的光合模式生物集胞藻属PCC 6803的膜协会使用蛋白质组学方法的相对紧密性。使用多个精确排名和实验验证的光合蛋白复合物的外周亚基作为地标，我们发现，参与双组分信号转导系统和转运蛋白的蛋白质整体上与膜紧密相关，而核糖体蛋白的关联要弱得多。此外，我们发现，假设的蛋白质含有相同的结构域通常具有相似的紧密性。这项工作提供了关于不同功能的膜蛋白质组结构组织的全局视图，并为未来研究响应不同环境或内部刺激的动态膜蛋白质组重组奠定了基础。
Large-scale quantitative evaluation of the tightness of membrane association for nontransmembrane proteins is important for identifying true peripheral membrane proteins with functional significance. Herein, we simultaneously ranked more than 1000 proteins of the photosynthetic model organism Synechocystis sp. PCC 6803 for their relative tightness of membrane association using a proteomic approach. Using multiple precisely ranked and experimentally verified peripheral subunits of photosynthetic protein complexes as the landmarks, we found that proteins involved in two-component signal transduction systems and transporters are overall tightly associated with the membranes, whereas the associations of ribosomal proteins are much weaker. Moreover, we found that hypothetical proteins containing the same domains generally have similar tightness. This work provided a global view of the structural organization of the membrane proteome with respect to divergent functions, and built the foundation for future investigation of the dynamic membrane proteome reorganization in response to different environmental or internal stimuli.