Thioredoxin: A Multifunctional Regulatory Protein with a Bright Future in Technology and Medicine

Buchanan, Bob B.; Schürmann, Peter; Decottignies, Paulette; Lozano, Rosa M.

doi:10.1006/abbi.1994.1439

Cited by 118 publications

(88 citation statements)

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“…Although sharing the unique active center sequence-Cys-Gly-Pro-Cys- (21,30), the two thioredoxins have a different phylogenetic history (6,(30)(31)(32). Thioredoxin-f selectively activates four of the five regulatory enzymes of the reductive pentose phosphate cycle, and thioredoxin-m activates NADP ϩ -malate dehydrogenase (9,33). Both thioredoxins are effective in activation of chloroplast ATP synthase (CF 1 -ATPase) (9).…”

Section: Discussionmentioning

confidence: 99%

“…Regulation via redox is an important mechanism characteristic of chloroplasts (5). Enzyme activities of the reductive pentose phosphate cycle in chloroplasts are regulated via a redox cascade generated by light (5)(6)(7)(8)(9). In the light, electrons from photosystem I are shuttled through the electron transport chain to ferredoxin and are transferred to thioredoxins by ferredoxin-thioredoxin reductase, and then to target enzymes, reducing a disulfide bond(s) of the enzymes and changing their catalytic activities.…”

Section: Concentration a Redox Cascade Is Likely To Link Between Ligmentioning

confidence: 99%

“…Synthesis of certain proteins in chloroplasts also is regulated via a redox cascade (10). In the redox cascade, thioredoxin acts as a transducer of redox potential generated by the light reactions of photosynthesis, providing the chloroplasts with a mechanism to coordinate the activity of various components of photosynthesis to the presence or absence of light (5)(6)(7)(8)(9).…”

Section: Concentration a Redox Cascade Is Likely To Link Between Ligmentioning

confidence: 99%

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Link between light and fatty acid synthesis: Thioredoxin-linked reductive activation of plastidic acetyl-CoA carboxylase

Sasaki

Kozaki

Hatano

1997

Proc. Natl. Acad. Sci. U.S.A.

161

124

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Fatty acid synthesis in chloroplasts is regulated by light. The synthesis of malonyl-CoA, which is catalyzed by acetyl-CoA carboxylase (ACCase) and is the first committed step, is modulated by light͞dark. Plants have ACCase in plastids and the cytosol. To determine the possible involvement of a redox cascade in light͞dark modulation of ACCase, the effect of DTT, a known reductant of S-S bonds, was examined in vitro for the partially purified ACCase from pea plant. Only the plastidic ACCase was activated by DTT. This enzyme was activated in vitro more efficiently by reduced thioredoxin, which is a transducer of redox potential during illumination, than by DTT alone. Chloroplast thioredoxin-f activated the enzyme more efficiently than thioredoxin-m. The ACCase also was activated by thioredoxin reduced enzymatically with NADPH and NADP-thioredoxin reductase. These findings suggest that the reduction of ACCase is needed for activation of the enzyme, and a redox potential generated by photosynthesis is involved in its activation through thioredoxin as for enzymes of the reductive pentose phosphate cycle. The catalytic activity of ACCase was maximum at pH 8 and 2-5 mM Mg 2؉ , indicating that light-produced changes in stromal pH and Mg 2؉ concentration modulate ACCase activity. These results suggest that light directly modulates a regulatory site of plastidic prokaryotic form of ACCase via a signal transduction pathway of a redox cascade and indirectly modulates its catalytic activity via stromal pH and Mg 2؉ concentration. A redox cascade is likely to link between light and fatty acid synthesis, resulting in coordination of fatty acid synthesis with photosynthesis.

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Section: Discussionmentioning

confidence: 99%

Section: Concentration a Redox Cascade Is Likely To Link Between Ligmentioning

confidence: 99%

Section: Concentration a Redox Cascade Is Likely To Link Between Ligmentioning

confidence: 99%

See 1 more Smart Citation

Link between light and fatty acid synthesis: Thioredoxin-linked reductive activation of plastidic acetyl-CoA carboxylase

Sasaki

Kozaki

Hatano

1997

Proc. Natl. Acad. Sci. U.S.A.

161

124

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“…Trx has a conserved role in the synthesis of DNA as a high-capacity hydrogen donor system for reducing the enzyme ribonucleotide reductase (Laurent et al 1964), the Met-SO and PAPS reductase (Tsang and Schiff 1976;Ejiri et al 1979). Thiol-redox control of Trx system also regulates chloroplast photosynthetic enzymes (Buchanan et al 1994). However, Trx can modulate the activity of proteins through protein-protein binding to signal molecules, such as apoptosis signal-regulating kinase 1 (ASK1).…”

Section: Thioredoxin Systemmentioning

confidence: 99%

Thioredoxin system – a novel therapeutic target

Koháryová¹,

Kollárová²

2015

gpb

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Abstract. Nowadays there are numerous pathogens that have created a resistance to commonly used antibiotics and drugs. Therefore research is focused on finding new therapeutic targets and on determination of their 3D structures that could help in designing new effective substances and inhibitors. Thioredoxin system not only plays a crucial role as thiol/disulfide redox controller, it is also essential for certain organisms as the only system ensuring the redox homeostasis. It is the redox-regulating function, which makes thioredoxin and thioredoxin reductase attractive for scientific research, especially in many studies of diseases caused by redox instability. Thanks to these facts, the proteins of thioredoxin system are suitable candidates for new therapeutic purposes. In this review we summarized the basic features of the thioredoxin system, we justified why the proteins of thioredoxin system are appropriate therapeutical targets and we provided overview of the possibilities of their inhibition by several types of inhibitors.

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“…Ferredoxin:thioredoxin reductase (FTR) is the key enzyme of the ferredoxin/thioredoxin system, the light-dependent enzyme regulatory system in oxygenic photosynthesis [1,2]. This nucleus-encoded enzyme reduces thioredoxins with electrons supplied through ferredoxin by illuminated thylakoids.…”

Section: Introductionmentioning

confidence: 99%

A dicistronic construct for the expression of functional spinach chloroplast ferredoxin:thioredoxin reductase in Escherichia coli

et al. 2000

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Ferredoxin:thioredoxin reductase (FTR) is a heterodimeric Fe S containing disulfide reductase involved in the light-dependent activation of photosynthetic enzymes. We have designed a dicistronic construct for the heterologous expression of this nucleus encoded chloroplast protein in Escherichia coli. The coding sequences for the two mature subunits have been inserted in tandem into the expression vector pET-3d. This dicistronic construct is correctly translated yielding soluble, perfectly functional FTR. The recombinant enzyme is composed of both subunits, contains the correctly inserted Fe S cluster as evidenced by its spectral properties and is indistinguishable from the enzyme isolated from leaves in its capacity to activate chloroplast fructose-1,6-bisphosphatase, one of the well known light activated enzymes of the Calvin cycle.

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Thioredoxin: A Multifunctional Regulatory Protein with a Bright Future in Technology and Medicine

Cited by 118 publications

References 0 publications

Link between light and fatty acid synthesis: Thioredoxin-linked reductive activation of plastidic acetyl-CoA carboxylase

Link between light and fatty acid synthesis: Thioredoxin-linked reductive activation of plastidic acetyl-CoA carboxylase

Thioredoxin system – a novel therapeutic target

A dicistronic construct for the expression of functional spinach chloroplast ferredoxin:thioredoxin reductase in Escherichia coli

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