铜绿假单胞菌SJTD-1的磷酸化蛋白质组学

Phosphoproteomics of Pseudomonas aeruginosa SJTD-1

制备了铜绿假单胞菌SJTD-1菌株的蛋白质组酶解产物,并利用二氧化钛磁珠从酶解产物中富集磷酸化肽.首次利用纳升液相色谱-质谱技术鉴定磷酸化肽的磷酸化位点,最终共鉴定获得13条磷酸化肽,分别来自12个磷酸化蛋白,其中有7个磷酸化蛋白在假单胞菌中是首次发现.分析鉴定到的磷酸化蛋白,发现大多与DNA复制、物质转运、能量代谢等密切相关.这是首次对铜绿假单胞菌SJTD-1菌株进行磷酸化蛋白质组学分析,为SJTD-1在DNA复制、物质和能量代谢以及细胞膜转运等方面的研究奠定基础.

SJTD-1,a novel kind of Pseudomonas aeruginosa,is isolated from oil-contaminated soil.It has been demonstrated that this bacterium can metabolize n-alkanes（C（12） to C（30））in our laboratory.Pseudomonas aeruginosa SJTD-1 may have wide applications in oil pollution.In our study,phosphopeptides of Pseudomonas aeruginosa SJTD-1 were enriched by TiO2 and 13 phosphopeptides from 12 phosphoproteins were first characterized by nano-liquid chromatography-mass spectrometry（nano LC-MS）.Among these identified phosphoproteins,7 phosphoproteins were first discovered in Pseudomonas aeruginosa.We found most of these identified phosphoproteins were related to DNA replication,material transport and energy metabolism.This is the first analysis of phosphorylation proteomic in Pseudomonas aeruginosa SJTD-1,and our results provide evidence for further research on DNA replication,material or energy metabolism and membrane transport in Pseudomonas aeruginosa.