scholarly journals The Novel ncRNA OsiR Positively Regulates Expression of katE2 and is Required for Oxidative Stress Tolerance in Deinococcus radiodurans

2020 ◽  
Vol 21 (9) ◽  
pp. 3200 ◽  
Author(s):  
Lihua Gao ◽  
Xiaonan Chen ◽  
Ye Tian ◽  
Yongliang Yan ◽  
Yuhua Zhan ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Stress Response ◽  
Stress Tolerance ◽  
Catalase Activity ◽  
Target Genes ◽  
Deinococcus Radiodurans ◽  
Oxidative Stress Response ◽  
Sequencing Analysis ◽  
Translation Efficiency ◽  
Oxidative Stress Tolerance

Deinococcus radiodurans is a polyextremophilic bacterium well known for its extreme resistance to irradiation, oxidative stress, and other damaging conditions. Many small noncoding RNAs (ncRNAs) in D. radiodurans have been identified by deep sequencing analysis and computational predictions. However, the precise roles of ncRNAs and their target genes in the oxidative stress response have not been investigated. Here, we report the identification and characterization of a novel ncRNA named OsiR (for oxidative stress-induced ncRNA). Oxidative stress tolerance analysis showed that deleting osiR significantly decreased viability, total antioxidant capacity, and catalase activity in D. radiodurans under oxidative stress conditions. Comparative phenotypic and qRT-PCR analyses of an osiR mutant identify a role of OsiR in regulating the expression of the catalase gene katE2. Microscale thermophoresis and genetic complementation showed that a 21-nt sequence in the stem–loop structure of OsiR (204–244 nt) directly base pairs with its counterpart in the coding region of katE2 mRNA (843–866 nt) via a 19 nt region. In addition, deletion of katE2 caused a significant reduction of catalase activity and oxidative stress tolerance similar to that observed in an osiR mutant. Our results show that OsiR positively regulates oxidative stress tolerance in D. radiodurans by increasing the mRNA stability and translation efficiency of katE2. This work provides a new regulatory pathway mediated by ncRNA for the oxidative stress response that most likely contributes to the extreme tolerances of D. radiodurans.

scholarly journals PICH, an ATP-dependent chromatin remodeling protein, transcriptionally co-regulates oxidative stress response.

2021 ◽  
Author(s):  
Anindita Dutta ◽  
Apurba Das ◽  
Deep Bisht ◽  
Vijendra Arya ◽  
Rohini Muthuswami
Keyword(s):  
Oxidative Stress ◽  
Transcription Factor ◽  
Transcriptional Regulation ◽  
Stress Response ◽  
Chromatin Remodeling ◽  
Dna Sequences ◽  
Target Genes ◽  
Antioxidant Response ◽  
Oxidative Stress Response ◽  
Antioxidant Genes

Cells respond to oxidative stress by elevating the levels of antioxidants, signaling, and transcriptional regulation often implemented by chromatin remodeling proteins.  The study presented in this paper shows that the expression of PICH, an ATP-dependent chromatin remodeler, is upregulated during oxidative stress in HeLa cells. We also show that PICH regulates the expression of Nrf2, a transcription factor regulating antioxidant response, both in the absence and presence of oxidative stress. In turn, Nrf2 regulates the expression of PICH in the presence of oxidative stress. Both PICH and Nrf2 together regulate the expression of antioxidant genes and this transcriptional regulation is dependent on the ATPase activity of PICH. In addition, H3K27ac modification also plays a role in activating transcription in the presence of oxidative stress. Co-immunoprecipitation experiments show that PICH and Nrf2 interact with H3K27ac in the presence of oxidative stress. Mechanistically, PICH recognizes ARE sequences present on its target genes and introduces a conformational change to the DNA sequences leading us to hypothesize that PICH regulates transcription by remodeling DNA. PICH ablation leads to reduced expression of Nrf2 and impaired antioxidant response leading to increased ROS content, thus, showing PICH is essential for the cell to respond to oxidative stress.

scholarly journals Catalase Expression inAzospirillum brasilenseSp7 Is Regulated by a Network Consisting of OxyR and Two RpoH Paralogs and Including an RpoE1→RpoH5 Regulatory Cascade

2018 ◽  
Vol 84 (23) ◽  
Author(s):  
Ashutosh Kumar Rai ◽  
Sudhir Singh ◽  
Sushil Kumar Dwivedi ◽  
Amit Srivastava ◽  
Parul Pandey ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Stress Response ◽  
Sinorhizobium Meliloti ◽  
Deinococcus Radiodurans ◽  
Oxidative Stress Response ◽  
Sigma Factors ◽  
Transcriptional Analysis ◽  
Content Type ◽  
Regulatory Cascade ◽  
Transcription Regulators

ABSTRACTThe genome ofAzospirillum brasilenseencodes five RpoH sigma factors: two OxyR transcription regulators and three catalases. The aim of this study was to understand the role they play during oxidative stress and their regulatory interconnection. Out of the 5 paralogs of RpoH present inA. brasilense, inactivation of onlyrpoH1rendersA. brasilenseheat sensitive. While transcript levels ofrpoH1were elevated by heat stress, those ofrpoH3andrpoH5were upregulated by H2O2. Catalase activity was upregulated inA. brasilenseand itsrpoH::kmmutants in response to H2O2except in the case of therpoH5::kmmutant, suggesting a role for RpoH5 in regulating inducible catalase. Transcriptional analysis of thekatN,katAI, andkatAII genes revealed that the expression ofkatNandkatAII was severely compromised in therpoH3::kmandrpoH5::kmmutants, respectively. Regulation ofkatNandkatAII by RpoH3 and RpoH5, respectively, was further confirmed in anEscherichia colitwo-plasmid system. Regulation ofkatAII by OxyR2 was evident by a drastic reduction in growth, KatAII activity, andkatAII::lacZexpression in anoxyR2::kmmutant. This study reports the involvement of RpoH3 and RpoH5 sigma factors in regulating oxidative stress response in alphaproteobacteria. We also report the regulation of an inducible catalase by a cascade of alternative sigma factors and an OxyR. Out of the three catalases inA. brasilense, those corresponding tokatNandkatAII are regulated by RpoH3 and RpoH5, respectively. The expression ofkatAII is regulated by a cascade of RpoE1→RpoH5 and OxyR2.IMPORTANCEIn silicoanalysis of theA. brasilensegenome showed the presence of multiple paralogs of genes involved in oxidative stress response, which included 2 OxyR transcription regulators and 3 catalases. So far,Deinococcus radioduransandVibrio choleraeare known to harbor two paralogs of OxyR, andSinorhizobium melilotiharbors three catalases. We do not yet know how the expression of multiple catalases is regulated in any bacterium. Here we show the role of multiple RpoH sigma factors and OxyR in regulating the expression of multiple catalases inA. brasilenseSp7. Our work gives a glimpse of systems biology ofA. brasilenseused for responding to oxidative stress.

scholarly journals TrmB, a tRNA m7G46 methyltransferase, plays a role in hydrogen peroxide resistance and positively modulates the translation of katA and katB mRNAs in Pseudomonas aeruginosa

2019 ◽  
Vol 47 (17) ◽  
pp. 9271-9281 ◽  
Author(s):  
Narumon Thongdee ◽  
Juthamas Jaroensuk ◽  
Sopapan Atichartpongkul ◽  
Jurairat Chittrakanwong ◽  
Kamonchanok Chooyoung ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Pseudomonas Aeruginosa ◽  
Stress Response ◽  
Translational Regulation ◽  
Cellular Response ◽  
Oxidative Stress Response ◽  
Translation Efficiency ◽  
Trna Modification ◽  
Negative Effect

Abstract Cellular response to oxidative stress is a crucial mechanism that promotes the survival of Pseudomonas aeruginosa during infection. However, the translational regulation of oxidative stress response remains largely unknown. Here, we reveal a tRNA modification-mediated translational response to H2O2 in P. aeruginosa. We demonstrated that the P. aeruginosa trmB gene encodes a tRNA guanine (46)-N7-methyltransferase that catalyzes the formation of m7G46 in the tRNA variable loop. Twenty-three tRNA substrates of TrmB with a guanosine residue at position 46 were identified, including 11 novel tRNA substrates. We showed that loss of trmB had a strong negative effect on the translation of Phe- and Asp-enriched mRNAs. The trmB-mediated m7G modification modulated the expression of the catalase genes katA and katB, which are enriched with Phe/Asp codons at the translational level. In response to H2O2 exposure, the level of m7G modification increased, consistent with the increased translation efficiency of Phe- and Asp-enriched mRNAs. Inactivation of trmB led to decreased KatA and KatB protein abundance and decreased catalase activity, resulting in H2O2-sensitive phenotype. Taken together, our observations reveal a novel role of m7G46 tRNA modification in oxidative stress response through translational regulation of Phe- and Asp-enriched genes, such as katA and katB.

scholarly journals Role of Heat Shock Transcription Factor in Saccharomyces cerevisiae Oxidative Stress Response

2007 ◽  
Vol 6 (8) ◽  
pp. 1373-1379 ◽  
Author(s):  
Ayako Yamamoto ◽  
Junko Ueda ◽  
Noritaka Yamamoto ◽  
Naoya Hashikawa ◽  
Hiroshi Sakurai
Keyword(s):  
Oxidative Stress ◽  
Saccharomyces Cerevisiae ◽  
Transcription Factor ◽  
Stress Response ◽  
Heat Shock ◽  
Superoxide Anion ◽  
Target Genes ◽  
Oxidative Stress Response ◽  
Heat Shock Transcription Factor ◽  
Negative Regulator

ABSTRACT The heat shock transcription factor Hsf1 of the yeast Saccharomyces cerevisiae regulates the transcription of a set of genes that contain heat shock elements (HSEs) in their promoters and function in diverse cellular processes, including protein folding. Here, we show that Hsf1 activates the transcription of various target genes when cells are treated with oxidizing reagents, including the superoxide anion generators menadione and KO2 and the thiol oxidants diamide and 1-chloro-2,4-dinitrobenzene (CDNB). Similar to heat shock, the oxidizing reagents are potent inducers of both efficient HSE binding and extensive phosphorylation of Hsf1. The inducible phosphorylation of Hsf1 is regulated by the intramolecular domain-domain interactions and affects HSE structure-specific transcription. Unlike the heat shock, diamide, or CDNB response, menadione or KO2 activation of Hsf1 is inhibited by cyclic-AMP-dependent protein kinase (PKA) activity, which negatively regulates the activator functions of other transcriptional regulators implicated in the oxidative stress response. These results demonstrate that Hsf1 is a member of the oxidative stress-responsive activators and that PKA is a general negative regulator in the superoxide anion response.

scholarly journals The BTB and CNC Homology 1 (BACH1) Target Genes Are Involved in the Oxidative Stress Response and in Control of the Cell Cycle

2011 ◽  
Vol 286 (26) ◽  
pp. 23521-23532 ◽  
Author(s):  
Hans-Jörg Warnatz ◽  
Dominic Schmidt ◽  
Thomas Manke ◽  
Ilaria Piccini ◽  
Marc Sultan ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Cell Cycle ◽  
Stress Response ◽  
Target Genes ◽  
Oxidative Stress Response

scholarly journals sRNA OsiA Stabilizes Catalase mRNA during Oxidative Stress Response of Deincoccus radiodurans R1

2019 ◽  
Vol 7 (10) ◽  
pp. 422 ◽  
Author(s):  
Yun Chen ◽  
Dong Xue ◽  
Wenjie Sun ◽  
Jiahui Han ◽  
Jiang Li ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Stress Response ◽  
Translational Regulation ◽  
Deinococcus Radiodurans ◽  
Extreme Environments ◽  
Oxidative Stress Response ◽  
Small Noncoding Rnas ◽  
Total Antioxidant ◽  
Increased Sensitivity ◽  
The Stability

Deinococcus radiodurans adapts to challenging environments by modulating gene expression in response to oxidative stress. Recently, bacterial small noncoding RNAs (sRNAs) have been presumed to participate in the transcriptional or translational regulation of stress-responsive genes. We found 24 sRNAs that may be involved in the oxidative stress response of D. radiodurans by deep RNA sequencing. Moreover, a typical stress-inducible sRNA, IGR_3053, named OsiA, was predicted to bind to the mRNA of katA, katE, and sodC by the bioinformatics method. An osiA knockout of D. radiodurans displayed increased sensitivity to H2O2 and the decreased catalase activity and total antioxidant activity, suggesting that OsiA probably serves as a regulator in the adaptation to oxidative environments. Further microscale thermophoresis results demonstrated that OsiA can directly bind to the mRNA of katA, sodC, and katE. The stability test result of katA mRNA showed that its half-life was 2 min in the osiA mutant compared with 5 min in the wildtype(wt) strain. Our results indicated that OsiA can enhance the stability of katA mRNA and the activity of KatA and consequently the oxidation resistance of D.radiodurans. We are the first one to explore the super-strong oxidative stress resistance of D.radiodurans at the level of post-transcriptional regulation, and found a new pathway that provides a new explanation for the long-term adaptability of D.radiodurans in extreme environments.

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