The bZIP transcription factor Afap1 mediates the oxidative stress response and aflatoxin biosynthesis in Aspergillus flavus.

The bZIP transcription factor Afap1 mediates the oxidative stress response and aflatoxin biosynthesis in Aspergillus flavus. Rev Argent Microbiol. 2019 Mar 21;: Authors: Guan X, Zhao Y, Liu X, Shang B, Xing F, Zhou L, Wang Y, Zhang C, Bhatnagar D, Liu Y Abstract Aflatoxin is a carcinogenic secondary metabolite produced mainly by Aspergillus flavus and Aspergillus parasiticus, which can seriously endanger the health of humans and animals. Oxidative stress is a common defense response, and it is known that reactive oxygen species (ROS) can induce the synthesis of a series of secondary metabolites, including aflatoxin. By using mutants lacking the afap 1 gene, the role of afap1 gene in oxidative stress and aflatoxin synthesis was assessed. The growth of the mutant strains was significantly inhibited by the increase in the concentration of H2O2, inhibition was complete at 40mmol/l. However, in the quantitative analysis by HPLC, the concentration of AFB1 increased with the increased H2O2 until 10mmol/l. Following an analysis based on the information provided by the NCBI BLAST analysis, it was assumed that Afap1, a basic leucine zipper (bZIP) transcription factor, was associated with the oxidative stress in this fungus. Treatment with 5mmol/l H2O2 completely inhibited the growth of the mutant strains in afap 1 but did not affect the growth of the CA14PTs strain (non-mutant strain). In addition, the concentration of AFB1 in the mutant strains was approximately &...
Source: Revista Argentina de Microbiologia - Category: Microbiology Tags: Rev Argent Microbiol Source Type: research

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Publication date: Available online 12 December 2019Source: Protein Expression and PurificationAuthor(s): Nisha Bhardwaj, Vijay Kumar Verma, Venkatesh Chaturvedi, Pradeep VermaAbstractIn the present investigation, cloning and overexpression of xylanase (XynF1), the main xylanase of A. oryzae LC1, was performed in prokaryotic system E. coli BL21(DE3) to produce recombinant xylanase with high titer of specific activity (1037.3 U/mg), which was 9.3-fold higher than the native strain. Further, the recombinant XynF1 of size 37 kDa was purified using Ni2+-NTA resins followed by cation exchange chromatography, which showed an 1....
Source: Protein Expression and Purification - Category: Biochemistry Source Type: research
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Source: Frontiers in Microbiology - Category: Microbiology Source Type: research
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