Journal of Microbiology

Journal Article

PprM is necessary for up-regulation of katE1, encoding the major catalase of Deinococcus radiodurans, under unstressed culture conditions: Sun-Wook Jeong , Ho Seong Seo , Min-Kyu Kim , Jong-Il Choi , Heon-Man Lim , Sangyong Lim; J. Microbiol. 2016;54(6):426-431. Published online May 27, 2016; DOI: https://doi.org/10.1007/s12275-016-6175-8

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Deinococcus radiodurans is a poly-extremophilic organism, capable of tolerating a wide variety of different stresses, such as gamma/ultraviolet radiation, desiccation, and oxidative stress. PprM, a cold shock protein homolog, is involved in the radiation resistance of D. radiodurans, but its role in the oxidative stress response has not been investigated. In this study, we investigated the effect of pprM mutation on catalase gene expression. pprM disruption decreased the mRNA and protein levels of KatE1, which is the major catalase in D. radiodurans, under normal culture conditions. A pprM mutant strain (pprMMT) exhibited decreased catalase activity, and its resistance to hydrogen peroxide (H2O2) decreased accordingly compared with that of the wild-type strain. We confirmed that RecG helicase negatively regulates katE1 under normal culture conditions. Among katE1 transcriptional regulators, the positive regulator drRRA was not altered in pprM-, while the negative regulators perR, dtxR, and recG were activated more than 2.5-fold in pprMMT. These findings suggest that PprM is necessary for KatE1 production under normal culture conditions by down-regulation of katE1 negative regulators.

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Antioxidant defense of Deinococcus radiodurans : how does it contribute to extreme radiation resistance?
Izabela Sadowska-Bartosz, Grzegorz Bartosz
International Journal of Radiation Biology.2023; 99(12): 1803. CrossRef
Development and Regulation of the Extreme Biofilm Formation of Deinococcus radiodurans R1 under Extreme Environmental Conditions
Qiannan Guo, Yuhua Zhan, Wei Zhang, Jin Wang, Yongliang Yan, Wenxiu Wang, Min Lin
International Journal of Molecular Sciences.2023; 25(1): 421. CrossRef
A small RNA regulates pprM, a modulator of pleiotropic proteins promoting DNA repair, in Deinococcus radiodurans under ionizing radiation
Jordan K. Villa, Runhua Han, Chen-Hsun Tsai, Angela Chen, Philip Sweet, Gabriela Franco, Respina Vaezian, Rok Tkavc, Michael J. Daly, Lydia M. Contreras
Scientific Reports.2021;[Epub] CrossRef
Lack of the Bacterial Phytochrome Protein Decreases Deinococcus radiodurans Resistance to Mitomycin C
Jong-Hyun Jung, Soyoung Jeong, Seonghun Im, Min-Kyu Kim, Ho Seong Seo, Sangyong Lim
Frontiers in Microbiology.2021;[Epub] CrossRef
Effects of Conserved Wedge Domain Residues on DNA Binding Activity of Deinococcus radiodurans RecG Helicase
Sun-Wook Jeong, Min-Kyu Kim, Lei Zhao, Seul-Ki Yang, Jong-Hyun Jung, Heon-Man Lim, Sangyong Lim
Frontiers in Genetics.2021;[Epub] CrossRef
The Novel ncRNA OsiR Positively Regulates Expression of katE2 and is Required for Oxidative Stress Tolerance in Deinococcus radiodurans
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International Journal of Molecular Sciences.2020; 21(9): 3200. CrossRef
Conservation and diversity of radiation and oxidative stress resistance mechanisms inDeinococcusspecies
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FEMS Microbiology Reviews.2019; 43(1): 19. CrossRef
Gene regulation for the extreme resistance to ionizing radiation of Deinococcus radiodurans
Wuzhou Wang, Yun Ma, Junyan He, Huizhou Qi, Fangzhu Xiao, Shuya He
Gene.2019; 715: 144008. CrossRef
PprM, a Cold Shock Domain-Containing Protein from Deinococcus radiodurans, Confers Oxidative Stress Tolerance to Escherichia coli
Sun-Ha Park, Harinder Singh, Deepti Appukuttan, Sunwook Jeong, Yong Jun Choi, Jong-Hyun Jung, Issay Narumi, Sangyong Lim
Frontiers in Microbiology.2017;[Epub] CrossRef
Knockout of pprM Decreases Resistance to Desiccation and Oxidation in Deinococcus radiodurans
Yang Zeng, Yun Ma, Fangzhu Xiao, Wuzhou Wang, Shuya He
Indian Journal of Microbiology.2017; 57(3): 316. CrossRef
RNA-Binding Domain is Necessary for PprM Function in Response to the Extreme Environmental Stress in Deinococcus radiodurans
Wei Li, Yun Ma, Jie Yang, Fangzhu Xiao, Wuzhou Wang, Shuya He
Indian Journal of Microbiology.2017; 57(4): 492. CrossRef

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Heat- and Cold-Shock Responses in Fusarium graminearum 3 Acetyl- and 15 Acetyl-Deoxynivalenol Chemotypes: Vladimir Vujanovic , Yit Kheng Goh , Prasad Daida; J. Microbiol. 2012;50(1):97-102. Published online February 27, 2012; DOI: https://doi.org/10.1007/s12275-012-1381-5

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Abstract: Fusarium graminearum Schwabe is the primary cause of Fusarium head blight (FHB) in North America. Chemically distinct F. graminearum sub-populations can be identified based on the type or composition of deoxynivalenol (DON) mycotoxin derivatives, including 3-acetyl (3-ADON) and 15-acetyl (15-ADON). The evaluation of randomly selected 3-ADON and 15-ADON isolates, collected from spring wheat throughout Canada, was performed using thin layer chromatography (TLC), high-performance liquid chromatography (HPLC), ice-nucleation activity (INA), and heat and cold tolerance tests conducted within a temperature range of -70°C to 65°C. The results indicated that the 3-ADON sub-population, which is responsible for the highest disease severity and has rapidly displaced the 15-ADON sub-population, produces more DON and zearalenone (ZEA) than the 15-ADON sub-population when exposed to heat and cold. Following exposures (1 and 2 h) to extremely high or low temperatures, 3-ADON isolates exhibited faster mycelial growth than 15-ADON isolates. In addition, the warmest temperature at which INA activity occurred was in 3-ADON (-3.6°C) vs. 15-ADON (-5.1°C). Taken together, these features suggest that the newly emerging 3-ADON sub-population is more resilient than the resident 15-ADON sub-population. Overall, the differences between the two sub-populations could provide new insights into FHB epidemiology and if validated under field conditions, may provide important information for predicting future FHB epidemics.

Rescue of a Cold-Sensitive Mutant at Low Temperatures by Cold Shock Proteins from Polaribacter irgensii KOPRI 22228: Ji-hyun Uh , Youn Hong Jung , Yoo Kyung Lee , Hong Kum Lee , Hana Im; J. Microbiol. 2010;48(6):798-802. Published online January 9, 2011; DOI: https://doi.org/10.1007/s12275-010-0402-5

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Abstract: Exposure to low temperatures induces the biosynthesis of specific sets of proteins, including cold shock proteins (Csps). Since many of the specific functions of pychrophilic Csps are unknown, the roles of Csps from an Arctic bacterium, Polaribacter irgensii KOPRI 22228, were examined. The genes encoding CspA and CspC of P. irgensii were cloned in this study. Sequence analysis showed that these proteins have cold shock domains containing two RNA-binding motifs, RNP1 and RNP2. Both proteins bound oligo(dT)-cellulose resins, suggesting single-stranded nucleic acid-binding activity. When the P. irgensii Csps were overexpressed in Escherichia coli, the cold-resistance of the host was increased by more than five-fold. The P. irgensii Csps also rescued a cold-sensitive E. coli csp-quadruple deletion strain, BX04, at low temperatures. These results suggest that Csps from P. irgensii play a role in survival in polar environments.

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