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Interaction of a Novel Zn2Cys6 Transcription Factor DcGliZ with Promoters in the Gliotoxin Biosynthetic Gene Cluster of the Deep-Sea-Derived Fungus Dichotomomyces cejpii.


ABSTRACT: Gliotoxin is an important epipolythiodioxopiperazine, which was biosynthesized by the gli gene cluster in Aspergillus genus. However, the regulatory mechanism of gliotoxin biosynthesis remains unclear. In this study, a novel Zn2Cys6 transcription factor DcGliZ that is responsible for the regulation of gliotoxin biosynthesis from the deep-sea-derived fungus Dichotomomyces cejpii was identified. DcGliZ was expressed in Escherichia coli and effectively purified from inclusion bodies by refolding. Using electrophoretic mobility shift assay, we demonstrated that purified DcGliZ can bind to gliG, gliM, and gliN promoter regions in the gli cluster. Furthermore, the binding kinetics and affinity of DcGliZ protein with different promoters were measured by surface plasmon resonance assays, and the results demonstrated the significant interaction of DcGliZ with the gliG, gliM, and gliN promoters. These new findings would lay the foundation for the elucidation of future gliotoxin biosynthetic regulation mechanisms in D. cejpii.

SUBMITTER: Huang ZL 

PROVIDER: S-EPMC7022936 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature

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Interaction of a Novel Zn2Cys6 Transcription Factor DcGliZ with Promoters in the Gliotoxin Biosynthetic Gene Cluster of the Deep-Sea-Derived Fungus <i>Dichotomomyces cejpii</i>.

Huang Zi-Lei ZL   Ye Wei W   Zhu Mu-Zi MZ   Kong Ya-Li YL   Li Sai-Ni SN   Liu Shan S   Zhang Wei-Min WM  

Biomolecules 20191229 1


Gliotoxin is an important epipolythiodioxopiperazine, which was biosynthesized by the <i>gli</i> gene cluster in <i>Aspergillus genus</i>. However, the regulatory mechanism of gliotoxin biosynthesis remains unclear. In this study, a novel Zn2Cys6 transcription factor DcGliZ that is responsible for the regulation of gliotoxin biosynthesis from the deep-sea-derived fungus <i>Dichotomomyces cejpii</i> was identified. DcGliZ was expressed in <i>Escherichia coli</i> and effectively purified from incl  ...[more]

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