PsTRXh1 and PsTRXh2 Are Both Pea h-Type Thioredoxins with Antagonistic Behavior in Redox Imbalances

Traverso, José Á.; Vignols, Florence; Cazalis, Roland; Pulido, Amada; Sahrawy, Mariam; Cejudo, Francisco Javier; Meyer, Yves; Chueca, Ana

doi:10.1104/pp.106.089524

Cited by 41 publications

(49 citation statements)

References 69 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In contrast, none of the Trxs h of group I identified in M. truncatula (h1-h3; Fig. 1) or known in pea (Montrichard et al, 2003;Traverso et al, 2007) has such a site. Isoforms of group I of M. truncatula have no predicted targeting sequence and may be cytosolic (Supplemental Table S1).…”

Section: Identification Of Trx H Sequences In M Truncatula Databasesmentioning

confidence: 91%

Identification and Characterization of Thioredoxin h Isoforms Differentially Expressed in Germinating Seeds of the Model Legume Medicago truncatula

et al. 2011

View full text Add to dashboard Cite

Thioredoxins (Trxs) h, small disulfide reductases, and NADP-thioredoxin reductases (NTRs) have been shown to accumulate in seeds of different plant species and play important roles in seed physiology. However, little is known about the identity, properties, and subcellular location of Trx h isoforms that are abundant in legume seeds. To fill this gap, in this work, we characterized the Trx h family of Medicago truncatula, a model legume, and then explored the activity and localization of Trx h isoforms accumulating in seeds. Twelve Trx h isoforms were identified in M. truncatula. They belong to the groups previously described: h1 to h3 (group I), h4 to h7 (group II), and h8 to h12 (group III). Isoforms of groups I and II were found to be reduced by M. truncatula NTRA, but with different efficiencies, Trxs of group II being more efficiently reduced than Trxs of group I. In contrast, their insulin disulfide-reducing activity varies greatly and independently of the group to which they belong. Furthermore, Trxs h1, h2, and h6 were found to be present in dry and germinating seeds. Trxs h1 and, to a lesser extent, h2 are abundant in both embryonic axes and cotyledons, while Trx h6 is mainly present in cotyledons. Thus, M. truncatula seeds contain distinct isoforms of Trx h that differ in spatial distribution and kinetic properties, suggesting that they play different roles. Because we show that Trx h6 is targeted to the tonoplast, the possible role of this isoform during germination is finally discussed.

show abstract

Section: Identification Of Trx H Sequences In M Truncatula Databasesmentioning

confidence: 91%

Identification and Characterization of Thioredoxin h Isoforms Differentially Expressed in Germinating Seeds of the Model Legume Medicago truncatula

et al. 2011

View full text Add to dashboard Cite

show abstract

“…The specificity of TRX h is currently under review. However, several studies based on yeast complementation, proteomics, and protein target identification methods have indicated important new functions for these cytosolic TRXs and suggested a role for these proteins in different stress situations (Mouaheb et al, 1998;Wong et al, 2004;Traverso et al, 2007). Several potential targets for TRX o proteins have emerged recently, but no specific function has yet been discovered for them .…”

mentioning

confidence: 99%

“…To date, one TRX f and two TRX m (m1 and m2) have been found in the chloroplast (Ló pez-Jaramillo et al, 1997;Pagano et al, 2000), and four TRX h are localized in the cytosol (Montrichard et al, 2003;Traverso et al, 2007). Both TRX f and TRX m regulate key enzymes that play an essential role in carbon fixation and sugar biosynthesis during photosynthesis.…”

mentioning

confidence: 99%

Localization in Roots and Flowers of Pea Chloroplastic Thioredoxin f and Thioredoxin m Proteins Reveals New Roles in Nonphotosynthetic Organs

et al. 2007

Self Cite

View full text Add to dashboard Cite

Plant thioredoxins (TRXs) are involved in redox regulation of a wide variety processes and usually exhibit organ specificity. We report strong evidence that chloroplastic TRXs are localized in heterotrophic tissues and suggest some ways in which they might participate in several metabolic and developmental processes. The promoter regions of the chloroplastic f and m1 TRX genes were isolated from a pea (Pisum sativum) plant genomic bank. Histochemical staining for b-glucuronidase (GUS) in transgenic homozygous Arabidopsis (Arabidopsis thaliana) plants showed preferential expression of the 444-bp PsTRXf1 promoter in early seedlings, stems, leaves, and roots, as well as in flowers, stigma, pollen grains, and filaments. GUS activity under the control of the 1,874-bp PsTRXm1 promoter was restricted to the leaves, roots, seeds, and flowers. To gain insight into the translational regulation of these genes, a series of deletions of 5# elements in both TRX promoters were analyzed. The results revealed that a 126-bp construct of the PsTRXf2 promoter was unable to reproduce the expression pattern observed with the full promoter. The differences in expression and tissue specificity between PsTRXm1 and the deleted promoters PsTRXm2 and PsTRXm3 suggest the existence of upstream positive or negative regulatory regions that affect tissue specificity, sucrose metabolism, and light regulation. PsTRXm1 expression is finely regulated by light and possibly by other metabolic factors. In situ hybridization experiments confirmed new localizations of these chloroplastic TRX transcripts in vascular tissues and flowers, and therefore suggest possible new functions in heterotrophic tissues related to cell division, germination, and plant reproduction.

show abstract

“…The Trx system appears to play a fundamental role in controlling redox status in animals and plants subjected to abiotic stress as Cd (Pagano et al 2000;Laloi et al 2004;Aina et al 2007;Traverso et al 2007). The oxidized form of Trx contains a disulfide (-S-S-) bridge that is reduced to the sulfhydryl state (-SH) via either reduced ferredoxin and ferredoxindependent thioredoxin reductase or NADPH and NTR (Balmer et al 2006;Jacquot et al 2009).…”

Section: Discussionmentioning

confidence: 99%

“…Moreover, the cosuppressed Arabidopsis lines lacking CDSP32 (two Trx domains) exhibit an increased sensitivity to oxidative stress (Broin and Rey 2003) and the expression of the cytosolic Trx h5 gene (AtTRXh5) is closely related to several oxidative stress situations (Laloi et al 2004). By the functional complementation of a Saccharomyces cerevisiae double mutant, Traverso et al (2007) have also demonstrated that Trx h1 and Trx h2 are involved in the control of (1) redox-imbalance and (2) hypersensitivity to hydrogen peroxide.…”

Section: Introductionmentioning

confidence: 99%

Cadmium affects the NADP-thioredoxin reductase/thioredoxin system in germinating pea seeds

Smiri

Jelali

Ghoul

2013

Journal of Plant Interactions

View full text Add to dashboard Cite

Seeds have devised sophisticated mechanisms to cope with adverse situations. Among these mechanisms the collectively referred to as redox homeostasis. We have investigated the thioredoxin (Trx)/NADPH/NADPHdependent thioredoxin reductase (NTR) systems during the pea (Pisum sativum L.) seed germination under heavy metal stress. Cotyledon and embryonic axis were analyzed between 0 and 5 days of germination in the presence or absence of cadmium (Cd). Under Cd stress conditions, NTR activity and Trx h3 and Trx h4 expression were stimulated, while the overall activity of Trx decreased. When incubated with Cd ions in vitro, the disulfide reductase activity of Trx h3 and f isoforms was drastically inhibited, probably through the formation of protein dimers as evidenced by the electrophoresis analysis. The NADPH status was also affected, since Cd treatment provoked an increase in oxidized state of coenzyme as compared to control redox ratio. The contribution of Trx system to the redox regulation during the germination is discussed in relation with the Cd-caused oxidative stress.

show abstract

PsTRXh1 and PsTRXh2 Are Both Pea h-Type Thioredoxins with Antagonistic Behavior in Redox Imbalances

Cited by 41 publications

References 69 publications

Identification and Characterization of Thioredoxin h Isoforms Differentially Expressed in Germinating Seeds of the Model Legume Medicago truncatula

Identification and Characterization of Thioredoxin h Isoforms Differentially Expressed in Germinating Seeds of the Model Legume Medicago truncatula

Localization in Roots and Flowers of Pea Chloroplastic Thioredoxin f and Thioredoxin m Proteins Reveals New Roles in Nonphotosynthetic Organs

Cadmium affects the NADP-thioredoxin reductase/thioredoxin system in germinating pea seeds

Contact Info

Product

Resources

About