4.6 Article

Transcriptome analysis and cytochrome P450 monooxygenase reveal the molecular mechanism of Bisphenol A degradation by Pseudomonas putida strain YC-AE1

期刊

BMC MICROBIOLOGY
卷 22, 期 1, 页码 -

出版社

BMC
DOI: 10.1186/s12866-022-02689-6

关键词

Bisphenol A; Pseudomonas putida YC-AE1; Cytochrome P450; Degradation pathway; RNA sequencing

资金

  1. National Natural Science Foundation of China
  2. Basic Research Fund of Chinese Academy of Agricultural Sciences [31540067, 21876201]
  3. [1610042017001]
  4. [1610042018005]
  5. [1610042018006]

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This study reveals the molecular mechanism and potential role of YC-AE1 cytochrome P450 monooxygenase in BPA degradation, and proposes the degradation pathway of BPA in YC-AE1.
Background: Bisphenol A (BPA) is a rapid spreading organic pollutant that widely used in many industries especially as a plasticizer in polycarbonate plastic and epoxy resins. BPA reported as a prominent endocrine disruptor compound that possesses estrogenic activity and fulminant toxicity. Pseudomonas putida YC-AE1 was isolated in our previous study and exerted a strong degradation capacity toward BPA at high concentrations; however, the molecular degradation mechanism is still enigmatic. Results: We employed RNA sequencing to analyze the differentially expressed genes (DEGs) in the YC-AE1 strain upon BPA induction. Out of 1229 differentially expressed genes, 725 genes were positively regulated, and 504 genes were down-regulated. The pathways of microbial metabolism in diverse environments were significantly enriched among DEGs based on KEGG enrichment analysis. qRT-PCR confirm the involvement of BPA degradation relevant genes in accordance with RNA Seq data. The degradation pathway of BPA in YC-AE1 was proposed with specific enzymes and encoded genes. The role of cytochrome P450 (CYP450) in BPA degradation was further verified. Sever decrease in BPA degradation was recorded by YC-AE1 in the presence of CYP450 inhibitor. Subsequently, CYP450bisdB deficient YC-AE1 strain delta bisdB lost its ability toward BPA transformation comparing with the wild type. Furthermore, Transformation of E. coli with pET-32a-bisdAB empowers it to degrade 66 mg l(-1) of BPA after 24 h. Altogether, the results showed the role of CYP450 in biodegradation of BPA by YC-AE1. Conclusion: In this study we propose the molecular basis and the potential role of YC-AE1cytochrome P450 monooxygenase in BPA catabolism.

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