Pap1p-dependent upregulation of thioredoxin 3 and thioredoxin reductase genes from the fission yeast under nitrosative stress

2012 ◽  
Vol 58 (2) ◽  
pp. 206-211 ◽  
Author(s):  
Min-Sik Park ◽  
Hyeon-Jung Kim ◽  
A Rum Park ◽  
Kisup Ahn ◽  
Hye-Won Lim ◽  
...  
2005 ◽  
Vol 4 (2) ◽  
pp. 487-489 ◽  
Author(s):  
Tricia A. Missall ◽  
Jennifer K. Lodge

ABSTRACT Thioredoxin reductase (TRR1) is an important component of the thioredoxin oxidative stress resistance pathway. Here we show that it is induced during oxidative and nitrosative stress and is preferentially localized to the mitochondria in Cryptococcus neoformans. The C. neoformans TRR1 gene encodes the low-molecular-weight isoform of the thioredoxin reductase enzyme, which shares little homology with that of its mammalian host. By replacing the endogenous TRR1 promoter with an inducible copper transporter promoter, we showed that Trr1 appears to be essential for viability of this pathogenic fungus, making it a potential antifungal target.


2004 ◽  
Vol 234 (2) ◽  
pp. 379-385 ◽  
Author(s):  
Sung-Min Hong ◽  
Hye-Won Lim ◽  
Il-Han Kim ◽  
Kanghwa Kim ◽  
Eun-Hee Park ◽  
...  

2021 ◽  
Author(s):  
Yana Shaulov ◽  
Lotem SARID ◽  
Meirav Trebicz-Geffen ◽  
Serge Ankri

Auranofin (AF), an antirheumatic agent, targets mammalian thioredoxin reductase (TrxR), an important enzyme controlling redox homeostasisis, AF is also very effective against a diversity of pathogenic bacteria and protozoan parasites. Here, we report about the resistance of the parasite Entamoeba histolytica to 2 microM of AF that has been acquired by gradual exposure of the parasite to increasing amount of the drug. AF adapted E.histolytica trophozoites (AFAT) has an impaired growth, cytopathic activity and they are more sensitive to oxidative stress (OS), nitrosative stress (NS) and metronidazole (MTZ) than wild type (WT) trophozoites. Integrated transcriptomics and redoxomics analyses showed that many upregulated genes in AFAT, including genes encoding for dehydrogenase and cytoskeletal proteins, have their product oxidized in wild type trophozoites exposed to AF (acute AF trophozoites) but not in AFAT. We also showed that the level of reactive oxygen species (ROS) and oxidized proteins (OXs) in AFAT is lower than that of acute AF trophozoites. Overexpression of E.histolytica TrxR (EhTrxR) did not protect the parasite against AF which suggests that EhTrxR is not central is the mechanism of adaptation to AF.


Antioxidants ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 1240
Author(s):  
Yana Shaulov ◽  
Lotem Sarid ◽  
Meirav Trebicz-Geffen ◽  
Serge Ankri

Auranofin (AF), an antirheumatic agent, targets mammalian thioredoxin reductase (TrxR), an important enzyme controlling redox homeostasis. AF is also highly effective against a diversity of pathogenic bacteria and protozoan parasites. Here, we report on the resistance of the parasite Entamoeba histolytica to 2 µM of AF that was acquired by gradual exposure of the parasite to an increasing amount of the drug. AF-adapted E. histolytica trophozoites (AFAT) have impaired growth and cytopathic activity, and are more sensitive to oxidative stress (OS), nitrosative stress (NS), and metronidazole (MNZ) than wild type (WT) trophozoites. Integrated transcriptomics and redoxomics analyses showed that many upregulated genes in AFAT, including genes encoding for dehydrogenase and cytoskeletal proteins, have their product oxidized in wild type trophozoites exposed to AF (acute AF trophozoites) but not in AFAT. We also showed that the level of reactive oxygen species (ROS) and oxidized proteins (OXs) in AFAT is lower than that in acute AF trophozoites. Overexpression of E. histolytica TrxR (EhTrxR) did not protect the parasite against AF, which suggests that EhTrxR is not central to the mechanism of adaptation to AF.


2006 ◽  
Vol 52 (12) ◽  
pp. 1261-1265 ◽  
Author(s):  
Nam-Chul Cho ◽  
Hyun-Jung Kang ◽  
Hye-Won Lim ◽  
Byung-Chul Kim ◽  
Eun-Hee Park ◽  
...  

To elicit the physiological roles of Pbh1, a baculoviral IAP repeat (BIR) domain-containing protein, in Schizosaccharomyces pombe, we investigated if Pbh1 expression is regulated by stress. The upstream region (1221 bp) of the pbh1 gene was fused into the promoterless β-galactosidase gene of the shuttle vector YEp367R, and the resultant fusion plasmid was named pPbh04. The synthesis of β-galactosidase from the pbh1-lacZ fusion gene was markedly enhanced by sodium nitroprusside (SNP) generating nitric oxide. The basal expression of the pbh1 gene required the presence of Pap1. Pap1 also mediated the induction of the pbh1 gene by SNP and nitrogen starvation. Pap1-dependent induction of the pbh1 gene by SNP was confirmed by the enhanced level of the pbh1 mRNA in Pap1-positive cells but not in Pap1-negative cells. Taken together, it was demonstrated that the pbh1 genes are positively regulated by nitrosative and nitrogen starvation stresses in Pap1-dependent manner.Key words: fission yeast, nitrosative stress, nutritional stress, nitrogen starvation, Pap1, Pbh1, regulation, Schizosaccharomyces pombe.


Author(s):  
Atsuko Shirai ◽  
Akihisa Matsuyama ◽  
Yoko Yashiroda ◽  
Ritsuko Arai ◽  
Minoru Yoshida

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