@article{mbs:/content/journal/micro/10.1099/mic.0.000139, author = "Karácsony, Zoltán and Gácser, Attila and Vágvölgyi, Csaba and Hamari, Zsuzsanna", title = "Further characterization of the role of the mitochondrial high-mobility group box protein in the intracellular redox environment of Aspergillus nidulans", journal= "Microbiology", year = "2015", volume = "161", number = "10", pages = "1897-1908", doi = "https://doi.org/10.1099/mic.0.000139", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.000139", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "HmbB, a predominantly mitochondrial high-mobility group box (HMGB) protein, of Aspergillus nidulans affects diverse biological activities, such as sterigmatocystin production, the maintenance of mitochondrial DNA copy number, germination of asexual and sexual spores, and protection against oxidative stress agents. We hypothesized that the latter correlates with an unbalanced intracellular redox state, in which case, a not yet fully characterized physiological function could be attributed to this mitochondrial HMGB protein. Here, we studied the intracellular redox environment and oxidative stress tolerance in hmbB + and hmbBΔ strains under normal and oxidative stress conditions by measuring glutathione redox couple, intracellular reactive oxygen species (ROS) content and ROS-protecting enzyme activities. Our results revealed that the intracellular redox environment is different in hmbBΔ conidia and mycelia from that of hmbB +, and shed light on the seemingly contradictory difference in the tolerance of hmbBΔ mycelia to diamide and menadione oxidative stressors.", }