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Analysis of Physiological Function of Escherichia coli Heme Peroxidase EfeB Based on Transcriptome / 中国生物化学与分子生物学报
Chinese Journal of Biochemistry and Molecular Biology ; (12): 772-777, 2022.
Artículo en Chino | WPRIM | ID: wpr-1015692
ABSTRACT
Heme peroxidase EfeB in E. coli belongs to the dye-decolorizing peroxidase (DyP) superfamily. Peroxidases in this superfamily have a good ability in degradation of synthetic dyes, but their physiological functions in organisms are unclear. In order to further understand the physiological function of EfeB, the mutant strain EcoΔefeB was constructed by homologous recombination. The differences between parental strain E. coli BL21 and EcoΔefeB at genome transcription level as well as cell growth under different conditions were compared. The response of efeB to iron ion was also investigated. The results showed that the deletion of efeB gene caused the differential expression of 1 765 genes, which were mainly related to cell metabolic pathway, cell membrane synthesis and flagellum movement. There was no significant difference in cell growth between BL21 and EcoΔefeB at pH 7. 0, but the growth of BL21 was much better than that of EcoΔefeB at pH 4. 5. The functional expression of efeB may support the survival of E. coli at low pH. EfeB was significantly up-regulated when Fe

Texto completo: Disponible Índice: WPRIM (Pacífico Occidental) Idioma: Chino Revista: Chinese Journal of Biochemistry and Molecular Biology Año: 2022 Tipo del documento: Artículo

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Texto completo: Disponible Índice: WPRIM (Pacífico Occidental) Idioma: Chino Revista: Chinese Journal of Biochemistry and Molecular Biology Año: 2022 Tipo del documento: Artículo