caa a22 4500 605501866 CHVBK 20210128100602.0 cr unu---uuuuu 210128e20150201xx s 000 0 eng 10.1007/s00253-014-6327-x doi (NATIONALLICENCE)springer-10.1007/s00253-014-6327-x Involvement of the NADH oxidase-encoding noxA gene in oxidative stress responses in Corynebacterium glutamicum [Elektronische Daten] [Jung Park, Younhee Kim, Heung-Shick Lee] Corynebacterium glutamicum ORF NCgl0328, designated noxA, encodes an NADH oxidase enzyme. The noxA gene, which was preferentially expressed in the log growth phase, was found to be under the control of the whcA, whcB, and whcE genes, which play regulatory roles in cells under oxidative stress. While noxA transcription was minimal in whcE-deleted mutant cells (ΔwhcE) during growth, its transcription was maximal even in the stationary phase in ΔwhcA cells. The transcription levels of noxA in ΔwhcB and whcB-overexpressing cells were comparable to the levels only in the log growth phase in ΔwhcA and whcA-overexpressing cells, respectively. Direct binding of purified WhcA to the promoter region of noxA was observed in vitro. The DNA-protein interaction was only possible in the presence of the reducing agent dithiothreitol. A noxA-deleted mutant strain and a strain overexpressing the noxA gene (P180-noxA) were established, and these strains were found to exhibit defective cell growth. The ΔnoxA and P180-noxA strains were sensitive to the redox-cycling oxidant menadione, suggesting a role of noxA in redox balancing. Accordingly, the purified NoxA enzyme exhibited NADH-oxidizing activity. Taken together, these data show that noxA plays a role in oxidative stress responses and also that the gene is under direct control of the WhcA protein, which was shown to be a regulatory DNA-binding protein. Furthermore, the involvement and roles of the whcA, whcB, and whcE genes in regulating the expression of noxA were demonstrated. Springer-Verlag Berlin Heidelberg, 2014 Corynebacterium glutamicum nationallicence whcA nationallicence whcB nationallicence whcE nationallicence NADH oxidase nationallicence Oxidative stress nationallicence Park Jung Department of Biotechnology and Bioinformatics, Korea University, 2511 Sejong-ro, 339-700, Sejong-si, Korea aut Kim Younhee Department of Oriental Medicine, Semyung University, 65 Semyung-ro, Jecheon-si, 390-711, Chungbuk, Korea aut Lee Heung-Shick Department of Biotechnology and Bioinformatics, Korea University, 2511 Sejong-ro, 339-700, Sejong-si, Korea aut Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/3(2015-02-01), 1363-1374 0175-7598 99:3<1363 2015 99 253 https://doi.org/10.1007/s00253-014-6327-x text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00253-014-6327-x text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Park Jung Department of Biotechnology and Bioinformatics, Korea University, 2511 Sejong-ro, 339-700, Sejong-si, Korea aut NATIONALLICENCE 700 1- Kim Younhee Department of Oriental Medicine, Semyung University, 65 Semyung-ro, Jecheon-si, 390-711, Chungbuk, Korea aut NATIONALLICENCE 700 1- Lee Heung-Shick Department of Biotechnology and Bioinformatics, Korea University, 2511 Sejong-ro, 339-700, Sejong-si, Korea aut NATIONALLICENCE 773 0- Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/3(2015-02-01), 1363-1374 0175-7598 99:3<1363 2015 99 253