A proteomic analysis of heterotrophic nitrifying bacterium Acinetobacter sp HITLi 7(T) adaptation to low temperature using two-dimensional difference gel electrophoresis approach
A proteomic analysis of heterotrophic nitrifying bacterium Acinetobacter sp HITLi 7(T) adaptation to low temperature using two-dimensional difference gel electrophoresis approach
复制标题
二维差异凝胶电泳对异养硝化细菌 Acinetobacter sp HITLi 7(T) 低温适应的蛋白质组学分析
DOI：
10.1016/j.ibiod.2016.03.009
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发表时间：
2016
影响因子：
4.8
通讯作者：
Song Yang
中科院分区：
文献类型：
--
作者：
Qin Wen;Li Wei-Guang;Huang Xiao-Fei;Zhang Duo-Ying;Song Yang
不动杆菌属。HITLi 7T在2℃下表现出异养硝化能力，最适生长温度为20℃，在2℃和20℃下，L−1h−1对氨氮的去除速率分别为0.09 mg和0.24 mg。菌体的生长和增殖对HITLi 7T的低温除氨性能有显著影响。为了研究低温对蛋白质表达的影响，用二维蛋白质组分析比较了HITLi 7T在2℃和20℃培养条件下的响应。经PDQuest 2D凝胶分析软件分析，共鉴定出151个差异表达蛋白。与20℃下的蛋白质表达相比，分别有17、28和43个蛋白质点在2℃下表达上调、下调和存在。利用基质辅助激光解吸电离飞行时间质谱仪成功地鉴定了9个在低温下过表达或诱导的斑点。在2℃时显著上调的蛋白质与代谢有关。仅在2℃下存在的蛋白质具有蛋白质生物合成和复性功能。这些结果表明，HITLi 7T的冷适应依赖于代谢途径的调节、蛋白质的合成和蛋白质的复性。
Acinetobactersp. HITLi 7Tshowed capacity of heterotrophic nitrification at 2 °C with an optimum growth temperature of 20 °C. The ammonium removal rates were 0.09 and 0.24 mg l−1h−1at 2 °C and 20 °C respectively. Cell growth and proliferation affected ammonium removal performance of HITLi 7Tdramatically at low temperature. To investigate the influence of low temperature on protein expression, the response of HITLi 7Tcultivated at 2 °C and 20 °C were characterized and compared by 2-dimensional proteome analyses. A total of 151 proteins were identified to be differentially expressed by the analysis of PDQuest 2D gel analysis software. In comparison to protein expression at 20 °C, 17, 28, and 43 protein spots were found to be up-regulated, down-regulated and only present at 2 °C, respectively. 9 spots, which were overexpressed or induced at low temperature, were successfully identified by peptide mass fingerprinting by matrix-assisted laser desorption ionization-time-of-flight mass spectrometry. The significantly up-regulated proteins at 2 °C were related to metabolism. The proteins only present at 2 °C had functions of protein biosynthesis and refolding. These findings indicated that cold adaption of HITLi 7Trelied on regulation of metabolic pathways, synthesis of proteins and protein refolding.