Chaperone-like properties of tobacco plastid thioredoxins f and m

Sanz-Barrio, Ruth; Millán, Alicia Fernández‐San; Carballeda, Jon; Corral-Martínez, Patricia; Seguí-Simarro, José M.; Farrán, Inmaculada

doi:10.1093/jxb/err282

Cited by 46 publications

(50 citation statements)

References 77 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Hence, the question of the nature of the physiological targets and roles of all these proteins should now be addressed using other approaches, such as the study of knockout and knockdown plants and in vivo or in vitro methods to identify protein partners. For instance, besides their usual disulfide reductase activity, it has recently been shown that some plastidial Trxs f and m have chaperone properties (Sanz-Barrio et al, 2012).…”

Section: Resultsmentioning

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

View full text Add to dashboard Cite

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.

show abstract

Section: Resultsmentioning

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

View full text Add to dashboard Cite

show abstract

“…Identification of catalase3 (AtCAT3) as one of the interacting proteins with GmTRX seems to support this scenario. Recent reports of the redox-independent, chaperone function of thioredoxins in E. coli, tobacco (N. tabacum), and Arabidopsis (Kern et al, 2003 ;Kthiri et al, 2008;Lee et al, 2009;Park et al, 2009;Sanz-Barrio et al, 2012) have provided a new insight into their diverse physiological roles. A novelty in our present finding is the potential role of GmTRX as a cytoplasmic chaperone largely specific for proteins targeted to peroxisomes.…”

Section: Discussionmentioning

confidence: 99%

“…Thermal aggregation of MDH was performed as described Park et al, 2009;Sanz-Barrio et al, 2012). MDH was incubated in 50 mM HEPES-KOH (pH 8.0) buffer at 43C with various concentrations of GmTRX (molar ratios of GmTRX to MDH of 1:1, 2:1 and 4:1).…”

Section: Chaperone Activitymentioning

confidence: 99%

“…Thus, the possibility that GmTRX may play a similar role as a chaperone was tested by assaying for holdase activity to reduce the thermal aggregation of malate dehydrogenase (MDH), as shown for other typical chaperones Park et al, 2009;Sanz-Barrio et al, 2012). Incubation of MDH with increasing amounts of GmTRX or GmTRX dm indeed prevented the thermal aggregation of MDH, which showed maximum protection at a molar ratio of 4 GmTRX (or GmTRX dm ) to 1 MDH ( Figs.…”

Section: Property Of Gmtrx As a Chaperonementioning

confidence: 99%

See 1 more Smart Citation

A Cytosolic Thioredoxin Acts as a Molecular Chaperone for Peroxisome Matrix Proteins as Well as Antioxidant in Peroxisome

Du¹,

Kim²,

Hur³

et al. 2015

Molecules and Cells

View full text Add to dashboard Cite

Thioredoxin (TRX) is a disulfide reductase present ubiquitously in all taxa and plays an important role as a regulator of cellular redox state. Recently, a redox-independent, chaperone function has also been reported for some thioredoxins. We previously identified nodulin-35, the subunit of soybean uricase, as an interacting target of a cytosolic soybean thioredoxin, GmTRX. Here we report the further characterization of the interaction, which turns out to be independent of the disulfide reductase function and results in the co-localization of GmTRX and nodulin-35 in peroxisomes, suggesting a possible function of GmTRX in peroxisomes. In addition, the chaperone function of GmTRX was demonstrated in in vitro molecular chaperone activity assays including the thermal denaturation assay and malate dehydrogenase aggregation assay. Our results demonstrate that the target of GmTRX is not only confined to the nodulin-35, but many other peroxisomal proteins, including catalase (AtCAT), transthyretin-like protein 1 (AtTTL1), and acyl-coenzyme A oxidase 4 (AtACX4), also interact with the GmTRX. Together with an increased uricase activity of nodulin-35 and reduced ROS accumulation observed in the presence of GmTRX in our results, especially under heat shock and oxidative stress conditions, it appears that GmTRX represents a novel thioredoxin that is co-localized to the peroxisomes, possibly providing functional integrity to peroxisomal proteins.

show abstract

“…Nevertheless, TRXm protein (Guelette et al, 2012; this study) and mRNA (Deeken et al, 2008) accumulate in phloem exudates, and TRXm1 and TRXm4 contribute to SAR (this work). How these proteins contribute to SAR remains to be determined, but recent evidence demonstrating the molecular holdase/foldase activity of NtTRXm in tobacco suggests that TRXm proteins act as molecular chaperones that protect target proteins during stress (Sanz-Barrio et al, 2012). As such, TRXm proteins may protect redox-sensitive proteins important for SAR in the phloem.…”

Section: Proteins Enriched In Sar-induced Phloem That Contribute To Tmentioning

confidence: 99%

Comparative Proteomics Analysis of Arabidopsis Phloem Exudates Collected During the Induction of Systemic Acquired Resistance

et al. 2016

View full text Add to dashboard Cite

ORCID IDs: 0000-0002-5467-7290 (P.C.); 0000-0002-3422-4083 (J.M.-P.).Systemic acquired resistance (SAR) is a plant defense response that provides long-lasting, broad-spectrum pathogen resistance to uninfected systemic leaves following an initial localized infection. In Arabidopsis (Arabidopsis thaliana), local infection with virulent or avirulent strains of Pseudomonas syringae pv tomato generates long-distance SAR signals that travel from locally infected to distant leaves through the phloem to establish SAR. In this study, a proteomics approach was used to identify proteins that accumulate in phloem exudates in response to the induction of SAR. To accomplish this, phloem exudates collected from mock-inoculated or SAR-induced leaves of wild-type Columbia-0 plants were subjected to label-free quantitative liquid chromatography-tandem mass spectrometry proteomics. Comparing mock-and SAR-induced phloem exudate proteomes, 16 proteins were enriched in phloem exudates collected from SAR-induced plants, while 46 proteins were suppressed. SAR-related proteins THIOREDOXIN h3, ACYL-COENZYME A-BINDING PROTEIN6, and PATHOGENESIS-RELATED1 were enriched in phloem exudates of SAR-induced plants, demonstrating the strength of this approach and suggesting a role for these proteins in the phloem during SAR. To identify novel components of SAR, transfer DNA mutants of differentially abundant phloem proteins were assayed for SAR competence. This analysis identified a number of new proteins (m-type thioredoxins, major latex protein-like protein, ULTRAVIOLET-B RESISTANCE8 photoreceptor) that contribute to the SAR response. The Arabidopsis SAR phloem proteome is a valuable resource for understanding SAR long-distance signaling and the dynamic nature of the phloem during plant-pathogen interactions.

show abstract

Chaperone-like properties of tobacco plastid thioredoxins f and m

Cited by 46 publications

References 77 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

A Cytosolic Thioredoxin Acts as a Molecular Chaperone for Peroxisome Matrix Proteins as Well as Antioxidant in Peroxisome

Comparative Proteomics Analysis of Arabidopsis Phloem Exudates Collected During the Induction of Systemic Acquired Resistance

Contact Info

Product

Resources

About