通过整合蛋白质组学和细菌双组分系统鉴定金传感肽
Identification of Gold Sensing Peptide by Integrative Proteomics and a Bacterial Two-Component System.
作者信息
Ng I-Son, Yu You-Jin, Yi Ying-Chen, Tan Shih-I, Huang Bo-Chuan, Han Yin-Lung
机构信息
Department of Chemical Engineering, National Cheng Kung University, Tainan, Taiwan.
Green Energy and Environment Research Laboratories, Natural Resources, Technology Division, Industrial Technology Research Institute, Hsinchu, Taiwan.
出版信息
Front Chem. 2017 Dec 22;5:127. doi: 10.3389/fchem.2017.00127. eCollection 2017.
The proteomics strategy was utilized to analyze and identify the gold adsorption proteins from AT-A2, due to its outstanding performance in gold-binding and recovery. The results showed that three small proteins, including histidine biosynthesis protein (HisIE), iron donor protein (CyaY) and hypothetical protein_65aa, have a higher ability to adsorb gold ions because of the negatively charged domains or metal binding sites. On the other hand, the PmrA/PmrB two-component system first replaces the iron (III)-binding motif using the peptide sequence from hypothetical protein_65aa, and this is then used to reveal the sensing and responsiveness to gold metal ions, which is totally different from the performance of traditional gold binding peptide (GBP) on the crystals on the surface of gold (111). We have successfully demonstrated an integrative proteomics and bacterial two-component system to explore the novel GBP. Finally, the heterologous over-expression of GBP by and the equilibrium of binding capacity for Au(III) have been conducted.
由于AT - A2在金结合和回收方面表现出色，采用蛋白质组学策略对其金吸附蛋白进行分析和鉴定。结果表明，包括组氨酸生物合成蛋白（HisIE）、铁供体蛋白（CyaY）和假定蛋白_65aa在内的三种小蛋白，因其带负电荷的结构域或金属结合位点而具有较高的金离子吸附能力。另一方面，PmrA/PmrB双组分系统首先利用假定蛋白_65aa的肽序列取代铁（III）结合基序，然后用于揭示对金金属离子的传感和响应，这与传统金结合肽（GBP）在金（111）表面晶体上的性能完全不同。我们成功地展示了一种综合蛋白质组学和细菌双组分系统来探索新型GBP。最后，进行了GBP的异源过表达以及对Au(III)结合能力的平衡研究。
Zotero 插件