The Ferredoxin/Thioredoxin System of Oxygenic Photosynthesis

Schürmann, Peter; Buchanan, Bob B.

doi:10.1089/ars.2007.1931

Cited by 380 publications

(368 citation statements)

References 320 publications

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“…Defining the oxidizing activity and the time at which it occurs could also be important for discerning the biological context of the redoxregulated phenomenon. Trx-regulated proteins are generally oxidized in the dark and are reduced upon illumination (Schürmann and Buchanan, 2008), but a Trx-implicated oxidizing activity was also found in the light (Trebitsh et al, 2000;Martinsuo et al, 2003), indicating a broader regulatory role for protein thiol oxidation.…”

Section: Introductionmentioning

confidence: 99%

“…If not regulated properly, the conversion of light energy into photosynthetic linear electron flow can turn in a short period of time into excessive production of deleterious reactive oxygen species (ROS). Perhaps because of the short time response needed, plants use photosynthetic redox signals as a direct and dynamic means to regulate multiple chloroplast phenomena, controlling the production of reducing equivalents and alleviating their inflicted damage (Karpinski et al, 1999;Trebitsh and Danon, 2001;Pfannschmidt, 2003;Rochaix, 2007;Schürmann and Buchanan, 2008). Yet, the mechanisms by which the redox signals are sensed are only beginning to unravel.…”

Section: Introductionmentioning

confidence: 99%

“…Nevertheless, a fraction of the reducing equivalents are transferred, for regulatory purposes, from ferredoxin via ferredoxin-dependent thioredoxin reductase to several chloroplast thioredoxins (Trxs). This reductive signal is then used by the Trxs to reduce disulfide bonds in regulatory sites of target chloroplast proteins, thereby modulating their activity (Schürmann and Buchanan, 2008;Meyer et al, 2009). In contrast with the photosynthetic reductive signal, the identity and mechanism of action of the oxidizing activity of the Trxregulated proteins are yet to be established.…”

Section: Introductionmentioning

confidence: 99%

“…Redox state changes of the plastoquinone pool regulate the reversible State I-State II transition phenomenon, redistributing the light capturing capacity between PSII and PSI and the phosphorylation of PSII proteins via the Ser/Thr protein kinases STN7 and STN8 (Allen et al, 1981;Zer et al, 1999;Bellafiore et al, 2005;Bonardi et al, 2005). In comparison, redox states of Trxs and the NADPH pool have been implicated in the coordination of stromal activity and in feedback regulation of the membranal reactions of photosynthesis (Johnson, 2003;Martinsuo et al, 2003;Hald et al, 2008;Schürmann and Buchanan, 2008). Several studies of the state transition phenomenon (Tikkanen et al, 2010), of the translation of the chloroplast psbA mRNA (Trebitsh et al, 2000;Trebitsh and Danon, 2001), and of chloroplast transcription (Pfannschmidt and Liere, 2005;Lemeille et al, 2009;Steiner et al, 2009) further suggested a cooperative regulation of the plastoquinone and the Trx pathways.…”

Section: Introductionmentioning

confidence: 99%

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A Chloroplast Light-Regulated Oxidative Sensor for Moderate Light Intensity in Arabidopsis

et al. 2012

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The transition from dark to light involves marked changes in the redox reactions of photosynthetic electron transport and in chloroplast stromal enzyme activity even under mild light and growth conditions. Thus, it is not surprising that redox regulation is used to dynamically adjust and coordinate the stromal and thylakoid compartments. While oxidation of regulatory proteins is necessary for the regulation, the identity and the mechanism of action of the oxidizing pathway are still unresolved. Here, we studied the oxidation of a thylakoid-associated atypical thioredoxin-type protein, ACHT1, in the Arabidopsis thaliana chloroplast. We found that after a brief period of net reduction in plants illuminated with moderate light intensity, a significant oxidation reaction of ACHT1 arises and counterbalances its reduction. Interestingly, ACHT1 oxidation is driven by 2-Cys peroxiredoxin (Prx), which in turn eliminates peroxides. The ACHT1 and 2-Cys Prx reaction characteristics in plants further indicated that ACHT1 oxidation is linked with changes in the photosynthetic production of peroxides. Our findings that plants with altered redox poise of the ACHT1 and 2-Cys Prx pathway show higher nonphotochemical quenching and lower photosynthetic electron transport infer a feedback regulatory role for this pathway.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

A Chloroplast Light-Regulated Oxidative Sensor for Moderate Light Intensity in Arabidopsis

et al. 2012

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“…Since the substrate affinities are not significantly altered by redox regulation (Table I), the inhibition appears to be caused mainly by reduction of the turnover number (k cat ). C-terminal extensions are known components of redox regulation in other chloroplast enzymes such as glyceraldehyde-3-phosphate dehydrogenase subunit B, Rubisco activase, or NADP-malate dehydrogenase (for review, see Schü rmann and Buchanan, 2008). For example, upon formation of a disulfide bond between two C-terminal Cys residues of the regulatory subunit of Rubisco activase, the C terminus impairs binding of ATP to the enzyme's P-loop domain (Portis et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

An Autoinhibitory Domain Confers Redox Regulation to Maize Glycerate Kinase

Bartsch

Mikkat²,

Hagemann

et al. 2010

Plant Physiology

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Glycerate 3-kinase (GLYK) is the terminal enzyme of the photorespiratory cycle in plants and many cyanobacteria. For several C 4 plants, notably grasses of the NADP-malic enzyme (ME) subtype, redox regulation of GLYK has been reported, but the responsible molecular mechanism is not known. We have analyzed the enzyme from the NADP-ME C 4 plant maize (Zea mays) and found that maize GLYK, in contrast to the enzyme from C 3 plants and a dicotyledonous NADP-ME C 4 plant, harbors a short carboxy-terminal extension. In its oxidized (night) form, a disulfide bridge is formed between the two cysteine residues present in this extra domain, and GLYK activity becomes inhibited. Cleavage of this bond by thioredoxin f produces the fully active thiol form, releasing autoinhibition. Fusion of the maize GLYK redox-regulatory domain to GLYK from C 3 plants confers redox regulation to these otherwise unregulated enzymes. It appears that redox regulation of GLYK could be an exclusive feature of monocotyledonous C 4 plants of the NADP-ME type, in which linear electron transport occurs only in the mesophyll chloroplasts. Hence, we suggest that GLYK, in addition to its function in photorespiration, provides glycerate 3-phosphate for the accelerated production of triose phosphate and its export from the mesophyll. This could facilitate the activation of redoxregulated Calvin cycle enzymes and the buildup of Calvin cycle intermediates in the bundle sheath of these particular C 4 plants during the dark/light transition.

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Genome‐wide analysis and transcriptional regulation of the typical and atypical thioredoxins in Arabidopsis thaliana

et al. 2021

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Thioredoxins (TRXs), a large subclass of ubiquitous oxidoreductases, are involved in thiol redox regulation. Here, we performed a comprehensive analysis of TRXs in the Arabidopsis thaliana genome, revealing 41 genes encoding 18 typical and 23 atypical TRXs, and 6 genes encoding thioredoxin reductases (TRs). The high number of atypical TRXs indicates special functions in plants that mostly await elucidation. We identified an atypical class of thioredoxins called TRX-c in the genomes of photosynthetic eukaryotes. Localized to the chloroplast, TRX-c displays atypical CPLC, CHLC and CNLC motifs in the active sites. In silico analysis of the transcriptional regulations of TRXs revealed high expression of TRX-c in leaves and strong regulation under cold, osmotic, salinity and metal ion stresses.

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The Ferredoxin/Thioredoxin System of Oxygenic Photosynthesis

Cited by 380 publications

References 320 publications

A Chloroplast Light-Regulated Oxidative Sensor for Moderate Light Intensity in Arabidopsis

A Chloroplast Light-Regulated Oxidative Sensor for Moderate Light Intensity in Arabidopsis

An Autoinhibitory Domain Confers Redox Regulation to Maize Glycerate Kinase

Genome‐wide analysis and transcriptional regulation of the typical and atypical thioredoxins in Arabidopsis thaliana

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