Using Quantitative Redox Proteomics to Dissect the Yeast Redoxome

Brandes, Nicolas; Reichmann, Dana; Tienson, Heather L.; Leichert, Lars I.; Jakob, Ursula

doi:10.1074/jbc.m111.296236

Cited by 108 publications

(117 citation statements)

References 54 publications

(20 reference statements)

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“…3B) (37,38). This method, termed as oxICAT, has been proven useful for determining changes in the extent of protein thiol oxidation in cells under stress conditions (37)(38)(39). oxICAT provides results that are unaffected by changes in the protein expression and stability.…”

Section: The Expanding Landscape Of the Thiol Redox Proteomementioning

confidence: 99%

The Expanding Landscape of the Thiol Redox Proteome

Yang

Carroll

Liebler

2016

Molecular & Cellular Proteomics

182

111

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Cysteine occupies a unique place in protein chemistry. The nucleophilic thiol group allows cysteine to undergo a broad range of redox modifications beyond classical thiol-disulfide redox equilibria, including S-sulfenylation (-SOH), S-sulfinylation (-SO 2 H), S-sulfonylation (-SO 3 H), S-nitrosylation (-SNO), S-sulfhydration (-SSH), S-glutathionylation (-SSG), and others. Emerging evidence suggests that these post-translational modifications (PTM) are important in cellular redox regulation and protection against oxidative damage. Identification of protein targets of thiol redox modifications is crucial to understanding their roles in biology and disease. However, analysis of these highly labile and dynamic modifications poses challenges. Recent advances in the design of probes for thiol redox forms, together with innovative mass spectrometry based chemoproteomics methods make it possible to perform global, site-specific, and quantitative analyses of thiol redox modifications in complex proteomes.

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Section: The Expanding Landscape Of the Thiol Redox Proteomementioning

confidence: 99%

The Expanding Landscape of the Thiol Redox Proteome

Yang

Carroll

Liebler

2016

Molecular & Cellular Proteomics

182

111

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“…Admittedly, targeted quantitative enrichment of thiol groups with OxICAT achieved better coverage of cysteine oxidation status, for example 400 different protein thiols in Saccharomyces cerevisiae (63) and thiol redox status for 140 proteins in Caenorhabditis elegans lifespan (64,65) were obtained. Even though powerful technologies to target large-scale methionine oxidation sites exist (66), they have not been applied to mitochondrial aging.…”

Section: Assessment Of the Untargeted Itraq-based Proteomic Approach mentioning

confidence: 99%

Global Protein Oxidation Profiling Suggests Efficient Mitochondrial Proteome Homeostasis During Aging

Guevara

Philipp

Hamann

et al. 2016

Molecular & Cellular Proteomics

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The free radical theory of aging is based on the idea that reactive oxygen species (ROS) may lead to the accumulation of age-related protein oxidation. Because the majority of cellular ROS is generated at the respiratory electron transport chain, this study focuses on the mitochondrial proteome of the aging model Podospora anserina as target for ROS-induced damage. To ensure the detection of even low abundant modified peptides, separation by long gradient nLC-ESI-MS/MS and an appropriate statistical workflow for iTRAQ quantification was developed. Artificial protein oxidation was minimized by establishing gel-free sample preparation in the presence of reducing and iron-chelating agents. This first large scale, oxidative modification-centric study for P. anserina allowed the comprehensive quantification of 22 different oxidative amino acid modifications, and notably the quantitative comparison of oxidized and nonoxidized protein species. In total 2341 proteins were quantified. For 746 both protein species (unmodified and oxidatively modified) were detected and the modification sites determined. The data revealed that methionine residues are preferably oxidized. Further prominent identified modifications in decreasing order of occurrence were carbonylation as well as formation of N-formylkynurenine and pyrrolidinone. Interestingly, for the majority of proteins a positive correlation of changes in protein amount and oxidative damage were noticed, and a general decrease in protein amounts at late age. However, it was discovered that few proteins changed in oxidative damage in accordance with former reports. Our data suggest that P. anserina is efficiently capable to counteract ROS-induced protein damage during aging as long as protein de novo synthesis is functioning, ultimately leading to an overall constant relationship between damaged and undamaged protein species. These findings contradict a massive increase in protein oxidation during aging and rather

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“…[112][113][114] Despite all of the great advantages that those sensors offer, some limitations can be pointed out. [115][116][117] HyPer and Amplex UltraRed are known to be pH sensitive, so precaution should be taken when measurements are in place. 115,116 The expression of these genetic tools in specific subcellular compartments can also disrupt the normal cellular environment.…”

Section: Ros-generating Proteins -Rgpsmentioning

confidence: 99%

Interplay between redox and protein homeostasis

Feleciano

Arnsburg

Kirstein

2016

Worm

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The subcellular compartments of eukaryotic cells are characterized by different redox environments. Whereas the cytosol, nucleus and mitochondria are more reducing, the endoplasmic reticulum represents a more oxidizing environment. As the redox level controls the formation of intra-and inter-molecular disulfide bonds, the folding of proteins is tightly linked to its environment. The proteostasis network of each compartment needs to be adapted to the compartmental redox properties. In addition to chaperones, also members of the thioredoxin superfamily can influence the folding of proteins by regulation of cysteine reduction/oxidation. This review will focus on thioredoxin superfamily members and chaperones of C. elegans, which play an important role at the interface between redox and protein homeostasis. Additionally, this review will highlight recent methodological developments on in vivo and in vitro assessment of the redox state and their application to provide insights into the high complexity of redox and proteostasis networks of C. elegans.

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Using Quantitative Redox Proteomics to Dissect the Yeast Redoxome

Cited by 108 publications

References 54 publications

The Expanding Landscape of the Thiol Redox Proteome

The Expanding Landscape of the Thiol Redox Proteome

Global Protein Oxidation Profiling Suggests Efficient Mitochondrial Proteome Homeostasis During Aging

Interplay between redox and protein homeostasis

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