2017 International Conference on Advanced Environmental Engineering | |
2-DE Compared with iTRAQ-based Proteomic Analysis of the Functional Regulation of Proteins in Rhodococcus sp. BAP-1 Response to Fluoranthene | |
生态环境科学 | |
Xu, Jie^1 ; Wang, Hongqi^1 ; Kong, Dekang^1 | |
Beijing Normal University, College of Water Sciences, Beijing, China^1 | |
关键词: Degradation pathways; Down-regulated proteins; Functional regulation; Innovative approaches; Methyltransferases; Polycyclic aromatic hydrocarbons (PAHS); Ribosomal proteins; Two-dimensional gel electrophoresis (2-DE); | |
Others : https://iopscience.iop.org/article/10.1088/1755-1315/111/1/012032/pdf DOI : 10.1088/1755-1315/111/1/012032 |
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学科分类:环境科学(综合) | |
来源: IOP | |
【 摘 要 】
Although the degradation pathways of Polycyclic aromatic hydrocarbons (PAHs) have been extensively studied in many bacteria, the variations in the expression levels of the key functional regulation of proteins during catabolism are still not quantitatively understood. In this study, we compared two proteomic methods, that one is two-dimensional gel electrophoresis (2-DE), a traditional widely used way and the other is isobaric tags for relative and absolute quantization (iTRAQ), an innovative approach, in order to analyze the functional regulation at the protein level in high effective fluoranthene-degrading bacteria named Rhodococcus sp. BAP-1. The number of differentially expressed proteins identified using iTRAQ is much larger than employing 2-DE. Response to fluoranthene, the key over expressed proteins in BAP-1 were NADPH-dependent FMN reductase, 30S ribosomal protein S2, S-ribosylhomocysteinase, etc.; the significant down-regulated proteins were cytochrome ubiquinol oxidase subunit, NAD(P) transhydrogenase subunit alpha, 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferase, et al.
【 预 览 】
Files | Size | Format | View |
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2-DE Compared with iTRAQ-based Proteomic Analysis of the Functional Regulation of Proteins in Rhodococcus sp. BAP-1 Response to Fluoranthene | 217KB | download |