Thiol-based H2O2 signalling in microbial systems

Boronat, Susanna; Domènech, Alba; Paulo, Esther; Calvo, Isabel A.; García-Santamarina, Sarela; Garcia, Patrícia Salomão; Dedo, Javier Encinar del; Barcons, Anna; Serrano, Érica Vieira; Carmona, Mercè; Hidalgo, Elena

doi:10.1016/j.redox.2014.01.015

Cited by 36 publications

(34 citation statements)

References 34 publications

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“…This reacts with its target protein, Yap1, forming inter‐protein disulfide bonds, which then resolve to produce Yap1 with an intra‐protein disulfide. Yap1 disulfide enters the nucleus where it acts as a transcription factor (Boronat et al ., ). Plants have a wide range of TPXs in most subcellular compartments, and it has been suggested that these could act as H 2 O 2 sensors.…”

Section: H2o2 Signallingmentioning

confidence: 97%

Hydrogen peroxide metabolism and functions in plants

2018

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1 I. Introduction 2 II. Measurement and imaging of H O 2 III. H O and O toxicity 3 IV. Production of H O : enzymes and subcellular locations 4 V. H O transport 9 VI. Control of H O concentration: how and where? 9 VII. Metabolic functions of H O 11 VIII. H O signalling 11 IX. Where next? 13 Acknowledgements 13 References 13 SUMMARY: Hydrogen peroxide (H O ) is produced, via superoxide and superoxide dismutase, by electron transport in chloroplasts and mitochondria, plasma membrane NADPH oxidases, peroxisomal oxidases, type III peroxidases and other apoplastic oxidases. Intracellular transport is facilitated by aquaporins and H O is removed by catalase, peroxiredoxin, glutathione peroxidase-like enzymes and ascorbate peroxidase, all of which have cell compartment-specific isoforms. Apoplastic H O influences cell expansion, development and defence by its involvement in type III peroxidase-mediated polymer cross-linking, lignification and, possibly, cell expansion via H O -derived hydroxyl radicals. Excess H O triggers chloroplast and peroxisome autophagy and programmed cell death. The role of H O in signalling, for example during acclimation to stress and pathogen defence, has received much attention, but the signal transduction mechanisms are poorly defined. H O oxidizes specific cysteine residues of target proteins to the sulfenic acid form and, similar to other organisms, this modification could initiate thiol-based redox relays and modify target enzymes, receptor kinases and transcription factors. Quantification of the sources and sinks of H O is being improved by the spatial and temporal resolution of genetically encoded H O sensors, such as HyPer and roGFP2-Orp1. These H O sensors, combined with the detection of specific proteins modified by H O , will allow a deeper understanding of its signalling roles.

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Section: H2o2 Signallingmentioning

confidence: 97%

Hydrogen peroxide metabolism and functions in plants

2018

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“…Interestingly, overexpression or increased nuclear accumulation of Pap1 also confers the resistance on S. pombe to various other agents such as staurosporine [110], caffeine [111], and berefeldin A [112] and to DNA damage in checkpoint deficient mutants [113]. Scavenging the tyrosyl radical in RNR may also generate the hydroperoxy radical form of HU [17], which diffuses away and directly or indirectly modifies Yap1, leading to its accumulation inside the nucleus and transcriptional activation of genes involved in the redox response [106,114]. The activated Aft regulon promotes iron uptake, which may exacerbate the oxidative stress via Fenton reaction [19,115].…”

Section: Accumulation Of Reactive Oxygen Species (Ros)mentioning

confidence: 99%

The Cell Killing Mechanisms of Hydroxyurea

Singh

2016

Genes

186

157

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Hydroxyurea is a well-established inhibitor of ribonucleotide reductase that has a long history of scientific interest and clinical use for the treatment of neoplastic and non-neoplastic diseases. It is currently the staple drug for the management of sickle cell anemia and chronic myeloproliferative disorders. Due to its reversible inhibitory effect on DNA replication in various organisms, hydroxyurea is also commonly used in laboratories for cell cycle synchronization or generating replication stress. However, incubation with high concentrations or prolonged treatment with low doses of hydroxyurea can result in cell death and the DNA damage generated at arrested replication forks is generally believed to be the direct cause. Recent studies in multiple model organisms have shown that oxidative stress and several other mechanisms may contribute to the majority of the cytotoxic effect of hydroxyurea. This review aims to summarize the progress in our understanding of the cell-killing mechanisms of hydroxyurea, which may provide new insights towards the improvement of chemotherapies that employ this agent.

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“…In yeast, the classical system supporting this model is the hydrogen peroxide signaling pathway controlled by the TF Yap1 from S. cerevisiae [248][249][250]. Yap1 is a basic leucine zipper (bZIP) TF that responds to hydrogen peroxide by activating the expression of genes for antioxidant enzymes and components of thiol homeostasis [251,258].…”

Section: Thiol-disulfide Exchange In Yeast Redox-sensing Transcriptiomentioning

confidence: 99%

“…Consequently, the Yap1-Crm1 complex is disrupted and Yap1 accumulates in the nucleus, leading to the activation of target genes (reviewed in Ref. [248]). Both Gpx3 and Yap1 are specifically reduced by the thioredoxin system upon removal of the stress, restoring the localization of Yap1 in the cytoplasm [249,253].…”

Section: Thiol-disulfide Exchange In Yeast Redox-sensing Transcriptiomentioning

confidence: 99%

Conferring specificity in redox pathways by enzymatic thiol/disulfide exchange reactions

Netto

Oliveira

Tairum

et al. 2016

Free Radical Research

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Thiol-disulfide exchange reactions are highly reversible, displaying nucleophilic substitutions mechanism (S(N)2 type). For aliphatic, low molecular thiols, these reactions are slow, but can attain million times faster rates in enzymatic processes. Thioredoxin (Trx) proteins were the first enzymes described to accelerate thiol-disulfide exchange reactions and their high reactivity is related to the high nucleophilicity of the attacking thiol. Substrate specificity in Trx is achieved by several factors, including polar, hydrophobic, and topological interactions through a groove in the active site. Glutaredoxin (Grx) enzymes also contain the Trx fold, but they do not share amino acid sequence similarity with Trx. A conserved glutathione binding site is a typical feature of Grx that can reduce substrates by two mechanisms (mono and dithiol). The high reactivity of Grx enzymes is related to the very acid pK(a) values of reactive Cys that plays roles as good leaving groups. Therefore, although distinct oxidoreductases catalyze similar thiol–disulfide exchange reactions, their enzymatic mechanisms vary. PDI and DsbA are two other oxidoreductases, but they are involved in disulfide bond formation, instead of disulfide reduction, which is related to the oxidative environment where they are found. PDI enzymes and DsbC are endowed with disulfide isomerase activity, which is related with their tetra-domain architecture. As illustrative description of specificity in thiol-disulfide exchange, redox aspects of transcription activation in bacteria, yeast, and mammals are presented in an evolutionary perspective. Therefore, thiol-disulfide exchange reactions play important roles in conferring specificity to pathways, a required feature for signaling.

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Thiol-based H2O2 signalling in microbial systems

Cited by 36 publications

References 34 publications

Hydrogen peroxide metabolism and functions in plants

Hydrogen peroxide metabolism and functions in plants

The Cell Killing Mechanisms of Hydroxyurea

Conferring specificity in redox pathways by enzymatic thiol/disulfide exchange reactions

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