Hybrids from pea chloroplast thioredoxins <i>f and m</i>: physicochemical and kinetic characteristics

Jaramillo, J. López; Chueca, Ana; Sahrawy, Mariam; Gorgé, J. López

doi:10.1046/j.1365-313x.1998.00176.x

Cited by 6 publications

(2 citation statements)

References 40 publications

(61 reference statements)

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“…Lopez-Jaramillo et al (22) reported similar results for hybrid proteins constructed between different types of chloroplastic thioredoxins. In both cases computer modeling indicated that these sequences are compatible with a normal stable thioredoxin folding.…”

Section: Model Of C Reinhardtii Thioredoxin H With a Wcppc Active Site-mentioning

confidence: 72%

Characterization of Determinants for the Specificity ofArabidopsis Thioredoxins h in Yeast Complementation

Bréhélin¹,

Mouaheb²,

Verdoucq³

et al. 2000

Journal of Biological Chemistry

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The disruption of the two thioredoxin genes in Saccharomyces cerevisiae leads to a complex phenotype, including the inability to use methionine sulfoxide as sulfur source, modified cell cycle parameters, reduced H 2 O 2 tolerance, and inability to use sulfate as sulfur source. Expression of one of the multiple Arabidopsis thaliana thioredoxins h in this mutant complements only some aspects of the phenotype, depending on the expressed thioredoxin: AtTRX2 or AtTRX3 induce methionine sulfoxide assimilation and restore a normal cell cycle. In addition AtTRX2 also confers growth on sulfate but no H 2 O 2 tolerance. In contrast, AtTRX3 does not confer growth on sulfate but induces H 2 O 2 tolerance. We have constructed hybrid proteins between these two thioredoxins and show that all information necessary for sulfate assimilation is present in the C-terminal part of AtTRX2, whereas some information needed for H 2 O 2 tolerance is located in the N-terminal part of AtTRX3. In addition, mutation of the atypical redox active site WCPPC to the classical site WCGPC restores some growth on sulfate. All these data suggest that the multiple Arabidopsis thioredoxins h originate from a totipotent ancestor with all the determinants necessary for interaction with the different thioredoxin target proteins. After duplications each member evolved by losing or masking some of the determinants.

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Section: Model Of C Reinhardtii Thioredoxin H With a Wcppc Active Site-mentioning

confidence: 72%

Characterization of Determinants for the Specificity ofArabidopsis Thioredoxins h in Yeast Complementation

Bréhélin¹,

Mouaheb²,

Verdoucq³

et al. 2000

Journal of Biological Chemistry

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“…Comparing the two structures from pea and spinach has revealed that large rearrangements are required to transform the oxidized inactive form into the reduced active form. Pea FBPase can be reactived efficiently by Trx f and to a lesser extent by pea Trx m and the double hybride Trx f/m, but not or very poorly by Trx x and y (Collin et al 2003(Collin et al , 2004Geck et al 1996, López-Jaramillo et al 1998. Unexpectedly, the activity of the chloroplastic fructose-1,6-bisphosphatase was also shown to be modulated in vitro by 2-Cys peroxiredoxin by an unknown process which does not seem to be related to the cysteines involved in the redox regulation (Caporaletti et al 2007).…”

Section: Fructose 16-biphosphatasementioning

confidence: 99%

The chloroplastic thiol reducing systems: dual functions in the regulation of carbohydrate metabolism and regeneration of antioxidant enzymes, emphasis on the poplar redoxin equipment

Chibani¹,

Couturier²,

Selles³

et al. 2009

Photosynth Res

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The post-translational modification consisting in the formation/reduction of disulfide bonds has been the subject of intense research in plants since the discovery in the 1970s that many chloroplastic enzymes are regulated by light through dithiol-disulfide exchange reactions catalyzed by oxidoreductases called thioredoxins (Trxs). Further biochemical and proteomic studies have considerably increased the number of target enzymes and processes regulated by these mechanisms in many sub-cellular compartments. Recently, glutathionylation, a modification consisting in the reversible formation of a glutathione adduct on cysteine residues, was proposed as an alternative redox regulation mechanism. Glutaredoxins (Grxs), proteins related to Trxs, are efficient catalysts for deglutathionylation, the opposite reaction. Hence, the Trxs- and Grxs-dependent pathways might constitute complementary and not only redundant regulatory processes. This article focuses on these two multigenic families and associated protein partners in poplar and on their involvement in the regulation of some major chloroplastic processes such as stress response, carbohydrate and heme/chlorophyll metabolism.

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Protein–Protein Interactions in Plant Thioredoxin Dependent Systems

Meyer

Miginiac‐Maslow

Schürmann

et al. 2018

Annual Plant Reviews Online

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Hybrids from pea chloroplast thioredoxins f and m: physicochemical and kinetic characteristics

Cited by 6 publications

References 40 publications

Characterization of Determinants for the Specificity ofArabidopsis Thioredoxins h in Yeast Complementation

Characterization of Determinants for the Specificity ofArabidopsis Thioredoxins h in Yeast Complementation

The chloroplastic thiol reducing systems: dual functions in the regulation of carbohydrate metabolism and regeneration of antioxidant enzymes, emphasis on the poplar redoxin equipment

Protein–Protein Interactions in Plant Thioredoxin Dependent Systems

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