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Proteomic analysis of Mortierella isabellina M6-22 during cold stress

机译:低温胁迫下伊莎伯氏菌M6-22的蛋白质组学分析

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We aimed to gain a better understanding of cold adaption in Mortierella isabellina M6-22 by using proteomics approaches. The temperature range and optimal temperature for M6-22 growth were investigated, and composition changes in fatty acids were analyzed. Accompanied with the 2-D gel electrophoresis, MALDI-TOF/TOFMS analysis was conducted to characterize alterations in protein profiling in M6-22 cultured at 30 degrees C for 24 h and 15 degrees C for another 24 h when compared with those cultured at 30 degrees C for 48 h. Gene Ontology (GO) cluster analysis was finally conducted for successfully identified proteins. M6-22 cells could grow well at temperatures ranging from 15 to 30 degrees C. As temperature decreased from 30 to 15 degrees C, LA and GLA significantly increased from 11.63 to 17.85 % and from 9.12 to 13.19 %, respectively, while oleic acid significantly decreased from 47.25 to 36.53 %. Proteomics analyses revealed 111 differentially expressed protein spots, among which 5 unique proteins (A38, A40, A47, A49 and A58), 29 up-regulated proteins and 10 down-regulated proteins were identified by MALDI-TOF/TOF-MS. GO enrichment analysis demonstrated that these proteins mainly involved in glycolytic pathway (A34 and A50), electron transport (A28), ATP production (A35 and B39) and protein modification (A38). A total of 44 differentially expressed proteins have been successfully identified in M. isabellina M6-22 cultured at 15 degrees C. These proteins may play important roles in cold adaption via regulation of ATP synthesis, activation of cold-adaptive proteins, degradation of needless protein, accumulation of PUFAs, etc.
机译:我们的目标是通过蛋白质组学方法更好地了解伊莎贝拉莫尔氏菌M6-22的冷适应能力。研究了M6-22生长的温度范围和最佳温度,并分析了脂肪酸的组成变化。与2-D凝胶电泳相结合,进行了MALDI-TOF / TOFMS分析,以表征与30℃下培养的M6-22在30℃下培养24 h和15℃下再培养24 h时蛋白质谱的变化。摄氏度48小时。最后,对成功鉴定出的蛋白质进行了基因本体(GO)聚类分析。 M6-22细胞可以在15至30摄氏度的温度下良好生长。随着温度从30摄氏度降至15摄氏度,LA和GLA分别从11.63%升高至17.85%和从9.12%升高至13.19%,而油酸显着提高从47.25降至36.53%。蛋白质组学分析揭示了111个差异表达的蛋白质斑点,其中MALDI-TOF / TOF-MS鉴定出5个独特的蛋白质(A38,A40,A47,A49和A58),29个上调蛋白质和10个下调蛋白质。 GO富集分析表明,这些蛋白质主要参与糖酵解途径(A34和A50),电子转运(A28),ATP产生(A35和B39)和蛋白质修饰(A38)。在15摄氏度下培养的伊萨伯氏菌M6-22中已成功鉴定出总共44种差异表达的蛋白质。这些蛋白质可能通过调节ATP合成,激活冷适应性蛋白质,降解不需要的蛋白质而在冷适应中发挥重要作用。 ,PUFA的积累等。

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