Influence of fadAG203R and ΔflbA Mutations on Morphology and Physiology of Submerged Aspergillus nidulans Cultures
Autor: | István Pócsi, Zsolt Molnár, Stefan Rosén, Edina Mészáros, Zsolt Szilágyi, Tamás Emri |
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Rok vydání: | 2004 |
Předmět: |
chemistry.chemical_classification
Reactive oxygen species Autolysis (biology) Protease biology medicine.medical_treatment fungi Mutant Bioengineering General Medicine biology.organism_classification Applied Microbiology and Biotechnology Biochemistry Microbiology Superoxide dismutase chemistry Catalase Aspergillus nidulans biology.protein medicine Energy source Molecular Biology Biotechnology |
Zdroj: | Applied Biochemistry and Biotechnology. 118:349-360 |
ISSN: | 0273-2289 |
DOI: | 10.1385/abab:118:1-3:349 |
Popis: | Morphologic and physiologic changes taking place in carbon-limited submerged cultures of Aspergillus nidulans ΔflbA and fadAG203R strains were studied. Loss-of-function mutation of the flbA gene resulted in an altered germination with unusually thick germination tubes, “fluffy” pellet morphology, as well as a reduced fragmentation rate of hyphae during autolysis. In the fadAG203R mutant strain, conidiophores formed in the stationary phase of growth, and the size of pellets shrank considerably. There were no significant differences in the generation of reactive oxygen species (ROS) and in the specific catalase and superoxide dismutase activities by the tested mutants and the appropriate parental strains. Therefore, the participation of ROS or antioxidative enzymes in FadA/FlbA signaling pathways seems to be unlikely in submerged cultures. On the other hand, earlier increases in the extracellular protease and ammonia production were recorded with the ΔflbA strain, whereas the protease and ammonia production of the fadAG203R mutant lagged behind those of the wild-type strains. Similar changes in the time courses of the induction of γ-glutamyltranspeptidase and the degradation of glutathione were observed. These results suggest that FadA/FlbA signaling may be involved in the mobilization of protein and peptide reserves as energy sources during carbon starvation. |
Databáze: | OpenAIRE |
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