20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: Implications for the degradation of oxidized proteins

Demasi, Marilene; Hand, Adrian; Ohara, Erina; Oliveira, Cristiano L. P.; Bicev, Renata N.; Bertoncini, Clélia Rejane Antônio; Netto, Luís Eduardo Soares

doi:10.1016/j.abb.2014.05.002

Cited by 18 publications

(9 citation statements)

References 41 publications

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“…One possible conclusion is that these systems are induced to clear oxidized proteins with the simultaneous induction of protein degradation and protein folding while protein synthesis is downregulated. Another possibility is that the induction of proteasome transcripts is a result of feedback, since the proteasome and the ubiquitin-activating/conjugating system have been shown to be inhibited by H 2 O 2 (Davies, 2001) and by glutathionylation (Demasi et al, 2014). The observed induction in protease transcripts may be responsible for the degradation of oxidatively damaged proteins in compartments and/or a means to compensate for reduced activity of the proteasome.…”

Section: Discussionmentioning

confidence: 99%

Genome‐wide analysis on Chlamydomonas reinhardtii reveals the impact of hydrogen peroxide on protein stress responses and overlap with other stress transcriptomes

et al. 2015

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SUMMARY Reactive oxygen species (ROS) are produced by and have the potential to be damaging to all aerobic organisms. In photosynthetic organisms, they are an unavoidable byproduct of electron transfer in both the chloroplast and mitochondrion. We employ the reference unicellular green alga, Chlamydomonas reinhardtii, to identify the effect of H2O2 on gene expression by monitoring the transcriptome changes in a timecourse experiment. Comparison of transcriptomes from cells sampled immediately prior to addition of H2O2, and 0.5 and 1 h subsequently revealed 1278 differentially abundant transcripts. Of those transcripts that increase in abundance, many encode proteins involved in ROS detoxification, protein degradation and stress-responses, whereas among those that decrease are transcripts encoding proteins involved in photosynthesis and central carbon metabolism. In addition to these transcriptomic adjustments, we observe that H2O2 addition is followed by an accumulation and oxidation of the total intracellular glutathione pool, and a decrease in photosynthetic O2 output. Additionally, we analyze our transcriptomes in the context of transcript abundance changes in response to singlet O2 (O2*), and relate our H2O2-induced transcripts to a diurnal transcriptome, where we demonstrate enrichments of H2O2-induced transcripts early in the light phase, late in the light phase and 2 h prior to light. On this basis several genes that are highlighted in this work may be involved in previously undiscovered stress remediation pathways or acclimation responses.

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Section: Discussionmentioning

confidence: 99%

Genome‐wide analysis on Chlamydomonas reinhardtii reveals the impact of hydrogen peroxide on protein stress responses and overlap with other stress transcriptomes

et al. 2015

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“…Examination of the S-glutathionylation state of the yeast proteasome revealed modified cysteine residues of the α5-subunit, of which Cys-76 is highly conserved from yeast to human. When this residue is S-glutathionylated, the 20S proteasome is in its maximal open gate conformation, increasing the accessibility for oxidized proteins (Silva et al, 2012; Demasi et al, 2014; Leme et al, 2019). Although the S-glutathionylated cysteine residues in the β-subunits could not be identified, S-glutathionylation of the proteasomal catalytic site promoted an allosteric modification, leading to changes in the length of the 20S proteasome, thereby probably inhibiting the ChT-L acticity (Silva et al, 2012).…”

Section: Proteasome Modulation By Post-translational Modificationsmentioning

confidence: 99%

Regulation of Proteasome Activity by (Post-)transcriptional Mechanisms

Kors

Geijtenbeek

Reits

et al. 2019

Front. Mol. Biosci.

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Intracellular protein synthesis, folding, and degradation are tightly controlled processes to ensure proper protein homeostasis. The proteasome is responsible for the degradation of the majority of intracellular proteins, which are often targeted for degradation via polyubiquitination. However, the degradation rate of proteins is also affected by the capacity of proteasomes to recognize and degrade these substrate proteins. This capacity is regulated by a variety of proteasome modulations including (1) changes in complex composition, (2) post-translational modifications, and (3) altered transcription of proteasomal subunits and activators. Various diseases are linked to proteasome modulation and altered proteasome function. A better understanding of these modulations may offer new perspectives for therapeutic intervention. Here we present an overview of these three proteasome modulating mechanisms to give better insight into the diversity of proteasomes.

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“…These seemingly opposing findings may be reconciled by the fact that oxidative stress is known to disengage the 20S core particle from the 19S regulatory unit, effectively increasing the pool of free 20S proteasome, which are capable of degrading proteins in an ATP-independent manner (Grune et al, 2011;Wang, Yen, Kaiser, & Huang, 2010). It has been proposed that this regulation evolved as an adaptive response to increased oxidative stress, enabling cells to increase their capacity to degrade oxidized proteins (Demasi et al, 2014(Demasi et al, , 2013. It is clear from this collection of studies that changes in redox and levels of S-glutathionylation have a direct impact on the activity of the proteasome; however, it is not clear if and how this affects the activity of Btz, or if this process contributes to the resistance phenotype in MM.…”

Section: Redox Signalingmentioning

confidence: 85%

Emerging Therapeutic Strategies for Overcoming Proteasome Inhibitor Resistance

Dolloff

2015

Advances in Cancer Research

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20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: Implications for the degradation of oxidized proteins

Cited by 18 publications

References 41 publications

Genome‐wide analysis on Chlamydomonas reinhardtii reveals the impact of hydrogen peroxide on protein stress responses and overlap with other stress transcriptomes

Genome‐wide analysis on Chlamydomonas reinhardtii reveals the impact of hydrogen peroxide on protein stress responses and overlap with other stress transcriptomes

Regulation of Proteasome Activity by (Post-)transcriptional Mechanisms

Emerging Therapeutic Strategies for Overcoming Proteasome Inhibitor Resistance

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