Plant Thioredoxin CDSP32 Regenerates 1-Cys Methionine Sulfoxide Reductase B Activity through the Direct Reduction of Sulfenic Acid

Tarrago, Lionel; Laugier, Edith; Zaffagnini, Mirko; Marchand, Christophe; Maréchal, Pierre Le; Lemaire, Stéphane D.; Rey, Pascal

doi:10.1074/jbc.m110.108373

Cited by 68 publications

(52 citation statements)

References 58 publications

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“…In the presence of GSH, it is most likely that the glutathionylated Trx form is resolved by another GSH molecule. This is different from the peculiar CDSP32, which can support the activity of AtMSRB1 without GSH by directly reducing the sulfenic acid formed on the catalytic Cys (Tarrago et al, 2010).…”

Section: Putative Physiological Targets Of Atypical Trxsmentioning

confidence: 99%

“…PrxIIB, PrxIIE, and MSRB1 are enzymes that use a single Cys residue in their catalytic cycle (Rouhier et al, 2002;Tarrago et al, 2009). The sulfenic acid formed upon catalysis is either reduced by GSH or directly by Trxs (Tarrago et al, 2009(Tarrago et al, , 2010. PtPrxQ, PtGpx1, PtGpx3, AtMSRB2, and PtMSRA4 are enzymes that form an intramolecular disulfide in the course of their catalysis Navrot et al, 2006;Tarrago et al, 2009).…”

Section: Regeneration Of Physiological Target Proteinsmentioning

confidence: 99%

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Atypical Thioredoxins in Poplar: The Glutathione-Dependent Thioredoxin-Like 2.1 Supports the Activity of Target Enzymes Possessing a Single Redox Active Cysteine

et al. 2012

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Plant thioredoxins (Trxs) constitute a complex family of thiol oxidoreductases generally sharing a WCGPC active site sequence. Some recently identified plant Trxs (Clot, Trx-like1 and -2, Trx-lilium1, -2, and -3) display atypical active site sequences with altered residues between the two conserved cysteines. The transcript expression patterns, subcellular localizations, and biochemical properties of some representative poplar (Populus spp.) isoforms were investigated. Measurements of transcript levels for the 10 members in poplar organs indicate that most genes are constitutively expressed. Using transient expression of green fluorescent protein fusions, Clot and Trx-like1 were found to be mainly cytosolic, whereas Trx-like2.1 was located in plastids. All soluble recombinant proteins, except Clot, exhibited insulin reductase activity, although with variable efficiencies. Whereas Trx-like2.1 and Trx-lilium2.2 were efficiently regenerated both by NADPH-Trx reductase and glutathione, none of the proteins were reduced by the ferredoxin-Trx reductase. Only Trx-like2.1 supports the activity of plastidial thiol peroxidases and methionine sulfoxide reductases employing a single cysteine residue for catalysis and using a glutathione recycling system. The second active site cysteine of Trx-like2.1 is dispensable for this reaction, indicating that the protein possesses a glutaredoxin-like activity. Interestingly, the Trx-like2.1 active site replacement, from WCRKC to WCGPC, suppresses its capacity to use glutathione as a reductant but is sufficient to allow the regeneration of target proteins employing two cysteines for catalysis, indicating that the nature of the residues composing the active site sequence is crucial for substrate selectivity/recognition. This study provides another example of the cross talk existing between the glutathione/glutaredoxin and Trx-dependent pathways.

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Section: Putative Physiological Targets Of Atypical Trxsmentioning

confidence: 99%

Section: Regeneration Of Physiological Target Proteinsmentioning

confidence: 99%

Atypical Thioredoxins in Poplar: The Glutathione-Dependent Thioredoxin-Like 2.1 Supports the Activity of Target Enzymes Possessing a Single Redox Active Cysteine

et al. 2012

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“…However, both in vitro (3) and in vivo (4), a group of enzymes called methionine sulfoxide reductases (Msr, EC 1.8.4.11) can use Trx as the electron donor to regenerate the oxidized proteins, by reducing Met-SO to methionine (5). Recently, the glutathione/glutaredoxin system has been discovered that it also could act as the electron donor for Met-SO reduction (6,7). This protective mechanism has been shown to play a significant role in elongating the lifespan of yeast, insects, and mammals (8 -10).…”

Section: Thioredoxins (Trxs)mentioning

confidence: 99%

“…Despite the fact that the three families have distinct differences in origin, structure, substrate specificity, and species distribution, they basically share a similar catalytic mechanism. The mechanism involves the oxidation of the catalytic cysteine to a sulfenic acid intermediate, followed by the formation of an intramolecular disulfide bond, and the final regeneration process driven by Trx or other reductants (6,7,(15)(16)(17)(18).…”

Section: Thioredoxins (Trxs)mentioning

confidence: 99%

Structural Plasticity of the Thioredoxin Recognition Site of Yeast Methionine S-Sulfoxide Reductase Mxr1

Guo

Shi

et al. 2011

Journal of Biological Chemistry

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The methionine S-sulfoxide reductase MsrA catalyzes the reduction of methionine sulfoxide, a ubiquitous reaction depending on the thioredoxin system. To investigate interactions between MsrA and thioredoxin (Trx), we determined the crystal structures of yeast MsrA/Mxr1 in their reduced, oxidized, and Trx2-complexed forms, at 2.03, 1.90, and 2.70 Å , respectively. Comparative structure analysis revealed significant conformational changes of the three loops, which form a plastic "cushion" to harbor the electron donor Trx2. The flexible C-terminal loop enabled Mxr1 to access the methionine sulfoxide on various protein substrates. Moreover, the plasticity of the Trx binding site on Mxr1 provides structural insights into the recognition of diverse substrates by a universal catalytic motif of Trx. Thioredoxins (Trxs)2 are ubiquitous small thiol-disulfide exchange proteins that are involved in many important cellular processes such as reduction of methionine sulfoxide, ribonucleotide, and peroxide (1). These proteins have a highly conserved active site of CXXC motif. During the reaction, the first Cys attacks the intramolecular disulfide bond in the substrate protein, accompanying w ith the formation of an intermolecular disulfide intermediate. This mixed disulfide is subsequently attacked by the second Cys, resulting in release of the reduced substrate protein and the oxidized Trx.

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“…The thiolate can also undergo thiol shuffling reactions (203) or react with H 2 O 2 to form a sulfenic (R-SOH) acid, also referred to as sulfenylation. Sulfenylation has been detected in the structural and mitochondrial proteins of cardiac myocytes treated with H 2 O 2 (46,241) and may be enzymatically reversed by Trx (277). At present, it is uncertain whether sulfenic acid can act as a signaling molecule, and speculation is that it acts as an intermediary for further oxidation only.…”

Section: Fig 4 Overview Compar-mentioning

confidence: 99%

Cardiovascular Redox and Ox Stress Proteomics

Kumar

Calamaras

Haeussler

et al. 2012

Antioxidants & Redox Signaling

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Significance: Oxidative post-translational modifications (OPTMs) have been demonstrated as contributing to cardiovascular physiology and pathophysiology. These modifications have been identified using antibodies as well as advanced proteomic methods, and the functional importance of each is beginning to be understood using transgenic and gene deletion animal models. Given that OPTMs are involved in cardiovascular pathology, the use of these modifications as biomarkers and predictors of disease has significant therapeutic potential. Adequate understanding of the chemistry of the OPTMs is necessary to determine what may occur in vivo and which modifications would best serve as biomarkers. Recent Advances: By using mass spectrometry, advanced labeling techniques, and antibody identification, OPTMs have become accessible to a larger proportion of the scientific community. Advancements in instrumentation, database search algorithms, and processing speed have allowed MS to fully expand on the proteome of OPTMs. In addition, the role of enzymatically reversible OPTMs has been further clarified in preclinical models. Critical Issues: The identification of OPTMs suffers from limitations in analytic detection based on the methodology, instrumentation, sample complexity, and bioinformatics. Currently, each type of OPTM requires a specific strategy for identification, and generalized approaches result in an incomplete assessment. Future Directions: Novel types of highly sensitive MS instrumentation that allow for improved separation and detection of modified proteins and peptides have been crucial in the discovery of OPTMs and biomarkers. To further advance the identification of relevant OPTMs in advanced search algorithms, standardized methods for sample processing and depository of MS data will be required. Antioxid. Redox Signal. 17, 1528-1559.

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Plant Thioredoxin CDSP32 Regenerates 1-Cys Methionine Sulfoxide Reductase B Activity through the Direct Reduction of Sulfenic Acid

Cited by 68 publications

References 58 publications

Atypical Thioredoxins in Poplar: The Glutathione-Dependent Thioredoxin-Like 2.1 Supports the Activity of Target Enzymes Possessing a Single Redox Active Cysteine

Atypical Thioredoxins in Poplar: The Glutathione-Dependent Thioredoxin-Like 2.1 Supports the Activity of Target Enzymes Possessing a Single Redox Active Cysteine

Structural Plasticity of the Thioredoxin Recognition Site of Yeast Methionine S-Sulfoxide Reductase Mxr1

Cardiovascular Redox and Ox Stress Proteomics

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