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Articles de revues sur le sujet « Thioredoxin »

Auteur : Grafiati

Publié le 4 juin 2021

Mis à jour le 25 mai 2024

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1

Langlotz, Petra, Wolfgang Wagner, and Hartmut Follmann. "Green Algae (Scenedesmus obliquus) Contain Three Thioredoxins of Regular Size." Zeitschrift für Naturforschung C 41, no. 11-12 (December 1, 1986): 979–87. http://dx.doi.org/10.1515/znc-1986-11-1205.

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Abstract A comprehensive thioredoxin profile of Scenedesmus obliquus has been established by chromatography of heat-stable protein extracts on five different ion exchange, gel permeation, and affinity chromatography columns and using three different assay systems including homologous S. obliquus ribonucleotide reductase, chloroplast fructose-bis-phosphatase, and NADP malate dehydrogenase. Four different thioredoxins were purified to homogeneity. Besides the large chloroplast thioredoxin f described previously, the algae contain three proteins of molecular weight 12,000 designated thioredoxin

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Nikkanen, Lauri, Jouni Toivola, Manuel Guinea Diaz, and Eevi Rintamäki. "Chloroplast thioredoxin systems: prospects for improving photosynthesis." Philosophical Transactions of the Royal Society B: Biological Sciences 372, no. 1730 (August 14, 2017): 20160474. http://dx.doi.org/10.1098/rstb.2016.0474.

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Thioredoxins (TRXs) are protein oxidoreductases that control the structure and function of cellular proteins by cleavage of a disulphide bond between the side chains of two cysteine residues. Oxidized thioredoxins are reactivated by thioredoxin reductases (TR) and a TR-dependent reduction of TRXs is called a thioredoxin system. Thiol-based redox regulation is an especially important mechanism to control chloroplast proteins involved in biogenesis, in regulation of light harvesting and distribution of light energy between photosystems, in photosynthetic carbon fixation and other biosynthetic pa

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Nikkanen, Lauri, and Eevi Rintamäki. "Thioredoxin-dependent regulatory networks in chloroplasts under fluctuating light conditions." Philosophical Transactions of the Royal Society B: Biological Sciences 369, no. 1640 (April 19, 2014): 20130224. http://dx.doi.org/10.1098/rstb.2013.0224.

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Plants have adopted a number of mechanisms to restore redox homeostasis in the chloroplast under fluctuating light conditions in nature. Chloroplast thioredoxin systems are crucial components of this redox network, mediating environmental signals to chloroplast proteins. In the reduced state, thioredoxins control the structure and function of proteins by reducing disulfide bridges in the redox active site of a protein. Subsequently, an oxidized thioredoxin is reduced by a thioredoxin reductase, the two enzymes together forming a thioredoxin system. Plant chloroplasts have versatile thioredoxin

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Cadet, F., and J. C. Meunier. "Spinach (Spinacia oleracea) chloroplast sedoheptulose-1,7-bisphosphatase. Activation and deactivation, and immunological relationship to fructose-1,6-bisphosphatase." Biochemical Journal 253, no. 1 (July 1, 1988): 243–48. http://dx.doi.org/10.1042/bj2530243.

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In this paper we study activation by dithiothreitol and reduced thioredoxins and deactivation by oxidized thioredoxins f of sedoheptulose-1,7-bisphosphatase. The behaviour of the enzyme when chromatographed on a thioredoxin-Sepharose column is also described. The enzyme is autoxidizable upon removal of reducing agents, and is activated when reduced by any of the thioredoxins. This mechanism may allow the regulation of the Calvin cycle upon light-dark and dark-light transitions. The formation of a stable complex between enzyme and thioredoxin could explain the inhibitory effect of high thioredo

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SERRATO, Antonio J., Juan M. PÉREZ-RUIZ, and Francisco J. CEJUDO. "Cloning of thioredoxin h reductase and characterization of the thioredoxin reductase–thioredoxin h system from wheat." Biochemical Journal 367, no. 2 (October 15, 2002): 491–97. http://dx.doi.org/10.1042/bj20020103.

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Thioredoxins h are ubiquitous proteins reduced by NADPH— thioredoxin reductase (NTR). They are able to reduce disulphides in target proteins. In monocots, thioredoxins h accumulate at high level in seeds and show a predominant localization in the nucleus of seed cells. These results suggest that the NTR—thioredoxin h system probably plays an important role in seed physiology. To date, the study of this system in monocots is limited by the lack of information about NTR. In the present study, we describe the cloning of a full-length cDNA encoding NTR from wheat (Triticum aestivum). The polypepti

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Langlotz, Petra, Wolfgang Wagner, and Hartmut Follmann. "A Large Chloroplast Thioredoxin ƒ Found in Green Algae." Zeitschrift für Naturforschung C 41, no. 3 (March 1, 1986): 275–83. http://dx.doi.org/10.1515/znc-1986-0306.

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Unicellular green algae differ from plant leaves in their thioredoxin profile. Besides several thioredoxins of regular size (Mr = 12,000), the heat-stable protein fraction of extracts from Scenedesmus obliquus cells contains a large protein of molecular weight Mr - 28,000 which is designated thioredoxin ƒ on the basis of typical properties, in particular by its capacity to stimulate spinach chloroplast fructose-bis-phosphatase and, to lower degree, E. coli ribonucleotide reductase. The new thioredoxin was purified to apparent homogeneity by chromatography on DEAE cellulose, Sephadex G-50. CM c

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Bodenstein, Johanna, and Hartmut Follmann. "Characterization of Two Thioredoxins in Pig Heart Including a New Mitochondrial Protein." Zeitschrift für Naturforschung C 46, no. 3-4 (April 1, 1991): 270–79. http://dx.doi.org/10.1515/znc-1991-3-418.

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Heart tissue contains two different thioredoxins. One is a specific mitochondrial protein and is best prepared from pre-isolated, intact heart mitochondria (mt-thioredoxin) whereas mitochondria-depleted tissue homogenates contain the major cellular thioredoxin of cytoplasmic origin (c-thioredoxin). Both heat-stable proteins are clearly differentiated chrom atographically. They exhibit slightly different molecular weights (12300 vs. 12000) and isoelectric points (4.7 vs. 4.8) but differ remarkably in their cysteine content: mt-Thioredoxin has two cysteine residues like the bacterial proteins, a

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Berndt, Carsten, Christopher Horst Lillig, and Arne Holmgren. "Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system." American Journal of Physiology-Heart and Circulatory Physiology 292, no. 3 (March 2007): H1227—H1236. http://dx.doi.org/10.1152/ajpheart.01162.2006.

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Reactive oxygen species (ROS) and the cellular thiol redox state are crucial mediators of multiple cell processes like growth, differentiation, and apoptosis. Excessive ROS production or oxidative stress is associated with several diseases, including cardiovascular disorders like ischemia-reperfusion. To prevent ROS-induced disorders, the heart is equipped with effective antioxidant systems. Key players in defense against oxidative stress are members of the thioredoxin-fold family of proteins. Of these, thioredoxins and glutaredoxins maintain a reduced intracellular redox state in mammalian ce

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Léveillard, Thierry, and Najate Aït-Ali. "Cell Signaling with Extracellular Thioredoxin and Thioredoxin-Like Proteins: Insight into Their Mechanisms of Action." Oxidative Medicine and Cellular Longevity 2017 (2017): 1–11. http://dx.doi.org/10.1155/2017/8475125.

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Thioredoxins are small thiol-oxidoreductase enzymes that control cellular redox homeostasis. Paradoxically, human thioredoxin (TXN1) was first identified as the adult T cell leukemia-derived factor (ADF), a secreted protein. ADF has been implicated in a wide variety of cell-to-cell communication systems acting as a cytokine or a chemokine. TRX80 is a truncated TXN1 protein with cytokine activity. The unconventional secretion mechanism of these extracellular thioredoxins is unknown. The thioredoxin system is relying on glucose metabolism through the pentose phosphate pathway that provides reduc

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Langlotz, Petra, and Hartmut Follmann. "Notes: Formation of Large Thioredoxin f Accompanies Chloroplast Development in Scenedesmus obliquus." Zeitschrift für Naturforschung C 42, no. 11-12 (December 1, 1987): 1364–66. http://dx.doi.org/10.1515/znc-1987-11-1241.

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Chloroplast-free mutant cells C-2A′ of the green algae Scenedesmus obliquus lack thioredoxin f, which functions in the light activation of chloroplast enzymes, but do contain the regular thioredoxins I and II. When dark-grown algae are transferred to light, thioredoxin f activity appears rapidly and increases in parallel with photosynthetic activities: however it precedes chlorophyll biosynthesis. The formation of thioredoxin f is inhibited by cydoheximide indicating that it occurs on the cytoplasmic ribosomes, in accord with the lack of thioredoxin genes on the chloroplast genomes.

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Rohrbach, Susanne, Stefanie Gruenler, Mirja Teschner, and Juergen Holtz. "The thioredoxin system in aging muscle: key role of mitochondrial thioredoxin reductase in the protective effects of caloric restriction?" American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 291, no. 4 (October 2006): R927—R935. http://dx.doi.org/10.1152/ajpregu.00890.2005.

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Cellular redox balance is maintained by various antioxidative systems. Among those is the thioredoxin system, consisting of thioredoxin, thioredoxin reductase, and NADPH. In the present study, we examined the effects of caloric restriction (2 mo) on the expression of the cytosolic and mitochondrial thioredoxin system in skeletal muscle and heart of senescent and young rats. Mitochondrial thioredoxin reductase (TrxR2) is significantly reduced in aging skeletal and cardiac muscle and renormalized after caloric restriction, while the cytosolic isoform remains unchanged. Thioredoxins (mitochondria

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Akif, Mohd, Garima Khare, Anil K. Tyagi, Shekhar C. Mande, and Abhijit A. Sardesai. "Functional Studies of Multiple Thioredoxins from Mycobacterium tuberculosis." Journal of Bacteriology 190, no. 21 (August 22, 2008): 7087–95. http://dx.doi.org/10.1128/jb.00159-08.

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ABSTRACT Cytoplasmic protein reduction via generalized thiol/disulfide exchange reactions and maintenance of cellular redox homeostasis is mediated by the thioredoxin superfamily of proteins. Here, we describe the characterization of the thioredoxin system from Mycobacterium tuberculosis, whose genome bears the potential to encode three putative thioredoxins from the open reading frames designated trxAMtb , trxBMtb , and trxCMtb . We show that all three thioredoxins, overproduced in Escherichia coli, are able to reduce insulin, a model substrate, in the presence of dithiothreitol. However, we

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Lunn, JE, A. Agostino, and MD Hatch. "Regulation of NADP-Malate Dehydrogenase in C4 Plants: Activity and Properties of Maize Thioredoxin M and the Significance of Non-Active Site Thiol Groups." Functional Plant Biology 22, no. 4 (1995): 577. http://dx.doi.org/10.1071/pp9950577.

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Some unusual properties of purified maize leaf thioredoxin m were attributable to the presence of non-active site thiol groups, Unlike thioredoxins from other sources, maize leaf thioredoxin m was susceptible to inactivation by heating and this was associated with polymerisation of the molecule. Both these effects of heating were prevented or reversed by adding thiol compounds such as dithiothreitol. We concluded that, on heating, the free SH groups in the oxidised thioredoxin m molecule react with disulfide groups of other molecules to form polymeric complexes linked by disulfide bonds. We al

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Smits, Wiep Klaas, Jean-Yves F. Dubois, Sierd Bron, Jan Maarten van Dijl, and Oscar P. Kuipers. "Tricksy Business: Transcriptome Analysis Reveals the Involvement of Thioredoxin A in Redox Homeostasis, Oxidative Stress, Sulfur Metabolism, and Cellular Differentiation in Bacillus subtilis." Journal of Bacteriology 187, no. 12 (June 15, 2005): 3921–30. http://dx.doi.org/10.1128/jb.187.12.3921-3930.2005.

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ABSTRACT Thioredoxins are important thiol-reactive proteins. Most knowledge about this class of proteins is derived from proteome studies, and little is known about the global transcriptional response of cells to various thioredoxin levels. In Bacillus subtilis, thioredoxin A is encoded by trxA and is essential for viability. In this study, we report the effects of minimal induction of a strain carrying an IPTG (isopropyl-β-d-thiogalactopyranoside)-inducible trxA gene (ItrxA) on transcription levels, as determined by DNA macroarrays. The effective depletion of thioredoxin A leads to the induct

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Gamiz-Arco, Gloria, Valeria A. Risso, Adela M. Candel, Alvaro Inglés-Prieto, Maria L. Romero-Romero, Eric A. Gaucher, Jose A. Gavira, Beatriz Ibarra-Molero, and Jose M. Sanchez-Ruiz. "Non-conservation of folding rates in the thioredoxin family reveals degradation of ancestral unassisted-folding." Biochemical Journal 476, no. 23 (December 10, 2019): 3631–47. http://dx.doi.org/10.1042/bcj20190739.

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Evolution involves not only adaptation, but also the degradation of superfluous features. Many examples of degradation at the morphological level are known (vestigial organs, for instance). However, the impact of degradation on molecular evolution has been rarely addressed. Thioredoxins serve as general oxidoreductases in all cells. Here, we report extensive mutational analyses on the folding of modern and resurrected ancestral bacterial thioredoxins. Contrary to claims from recent literature, in vitro folding rates in the thioredoxin family are not evolutionarily conserved, but span at least

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Trotter, Eleanor W., and Chris M. Grant. "Overlapping Roles of the Cytoplasmic and Mitochondrial Redox Regulatory Systems in the Yeast Saccharomyces cerevisiae." Eukaryotic Cell 4, no. 2 (February 2005): 392–400. http://dx.doi.org/10.1128/ec.4.2.392-400.2005.

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ABSTRACT Thioredoxins are small, highly conserved oxidoreductases which are required to maintain the redox homeostasis of the cell. Saccharomyces cerevisiae contains a cytoplasmic thioredoxin system (TRX1, TRX2, and TRR1) as well as a complete mitochondrial thioredoxin system, comprising a thioredoxin (TRX3) and a thioredoxin reductase (TRR2). In the present study we have analyzed the functional overlap between the two systems. By constructing mutant strains with deletions of both the mitochondrial and cytoplasmic systems (trr1 trr2 and trx1 trx2 trx3), we show that cells can survive in the ab

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Viefhues, Anne, Jens Heller, Nora Temme, and Paul Tudzynski. "Redox Systems in Botrytis cinerea: Impact on Development and Virulence." Molecular Plant-Microbe Interactions® 27, no. 8 (August 2014): 858–74. http://dx.doi.org/10.1094/mpmi-01-14-0012-r.

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The thioredoxin system is of great importance for maintenance of cellular redox homeostasis. Here, we show that it has a severe influence on virulence of Botrytis cinerea, demonstrating that redox processes are important for host-pathogen interactions in this necrotrophic plant pathogen. The thioredoxin system is composed of two enzymes, the thioredoxin and the thioredoxin reductase. We identified two genes encoding for thioredoxins (bctrx1, bctrx2) and one gene encoding for a thioredoxin reductase (bctrr1) in the genome of B. cinerea. Knockout mutants of bctrx1 and bctrr1 were severely impair

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Seco-Cervera, Marta, Pilar González-Cabo, Federico Pallardó, Carlos Romá-Mateo, and José García-Giménez. "Thioredoxin and Glutaredoxin Systems as Potential Targets for the Development of New Treatments in Friedreich’s Ataxia." Antioxidants 9, no. 12 (December 10, 2020): 1257. http://dx.doi.org/10.3390/antiox9121257.

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The thioredoxin family consists of a small group of redox proteins present in all organisms and composed of thioredoxins (TRXs), glutaredoxins (GLRXs) and peroxiredoxins (PRDXs) which are found in the extracellular fluid, the cytoplasm, the mitochondria and in the nucleus with functions that include antioxidation, signaling and transcriptional control, among others. The importance of thioredoxin family proteins in neurodegenerative diseases is gaining relevance because some of these proteins have demonstrated an important role in the central nervous system by mediating neuroprotection against

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Jakupoglu, Cemile, Gerhard K. H. Przemeck, Manuela Schneider, Stéphanie G. Moreno, Nadja Mayr, Antonis K. Hatzopoulos, Martin Hrabé de Angelis, et al. "Cytoplasmic Thioredoxin Reductase Is Essential for Embryogenesis but Dispensable for Cardiac Development." Molecular and Cellular Biology 25, no. 5 (March 1, 2005): 1980–88. http://dx.doi.org/10.1128/mcb.25.5.1980-1988.2005.

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ABSTRACT Two distinct thioredoxin/thioredoxin reductase systems are present in the cytosol and the mitochondria of mammalian cells. Thioredoxins (Txn), the main substrates of thioredoxin reductases (Txnrd), are involved in numerous physiological processes, including cell-cell communication, redox metabolism, proliferation, and apoptosis. To investigate the individual contribution of mitochondrial (Txnrd2) and cytoplasmic (Txnrd1) thioredoxin reductases in vivo, we generated a mouse strain with a conditionally targeted deletion of Txnrd1. We show here that the ubiquitous Cre-mediated inactivati

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Sytykiewicz, Hubert, Iwona Łukasik, Sylwia Goławska, Iwona Sprawka, Artur Goławski, Julia Sławianowska, and Katarzyna Kmieć. "Expression of Thioredoxin/Thioredoxin Reductase System Genes in Aphid-Challenged Maize Seedlings." International Journal of Molecular Sciences 21, no. 17 (August 31, 2020): 6296. http://dx.doi.org/10.3390/ijms21176296.

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Thioredoxins (Trxs) and thioredoxin reductases (TrxRs) encompass a highly complex network involved in sustaining thiol-based redox homeostasis in plant tissues. The purpose of the study was to gain a new insight into transcriptional reprogramming of the several genes involved in functioning of Trx/TrxR system in maize (Zea mays L.) seedlings, exposed to the bird cherry-oat aphid (Rhopalosiphum padi L.) or the rose-grass aphid (Metopolophium dirhodum Walk.) infestation. The biotests were performed on two maize genotypes (susceptible Złota Karłowa and relatively resistant Waza). The application

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Buey, Rubén M., David Fernández-Justel, Gloria González-Holgado, Marta Martínez-Júlvez, Adrián González-López, Adrián Velázquez-Campoy, Milagros Medina, Bob B. Buchanan, and Monica Balsera. "Unexpected diversity of ferredoxin-dependent thioredoxin reductases in cyanobacteria." Plant Physiology 186, no. 1 (February 18, 2021): 285–96. http://dx.doi.org/10.1093/plphys/kiab072.

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Abstract Thioredoxin reductases control the redox state of thioredoxins (Trxs)—ubiquitous proteins that regulate a spectrum of enzymes by dithiol–disulfide exchange reactions. In most organisms, Trx is reduced by NADPH via a thioredoxin reductase flavoenzyme (NTR), but in oxygenic photosynthetic organisms, this function can also be performed by an iron-sulfur ferredoxin (Fdx)-dependent thioredoxin reductase (FTR) that links light to metabolic regulation. We have recently found that some cyanobacteria, such as the thylakoid-less Gloeobacter and the ocean-dwelling green oxyphotobacterium Prochlo

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Lee, Hang-mao, Karl Josef Dietz, and Ralf Hofestädt. "Prediction of thioredoxin and glutaredoxin target proteins by identifying reversibly oxidized cysteinyl residues." Journal of Integrative Bioinformatics 7, no. 3 (December 1, 2010): 208–18. http://dx.doi.org/10.1515/jib-2010-130.

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Summary A significant part of cellular proteins undergo reversible thiol-dependent redox transitions which often control or switch protein functions. Thioredoxins and glutaredoxins constitute two key players in this redox regulatory protein network. Both interact with various categories of proteins containing reversibly oxidized cysteinyl residues. The identification of thioredoxin/glutaredoxin target proteins is a critical step in constructing the redox regulatory network of cells or subcellular compartments. Due to the scarcity of thioredoxin/glutaredoxin target protein records in the public

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Achard, Maud E. S., Amanda J. Hamilton, Tarek Dankowski, Begoña Heras, Mark S. Schembri, Jennifer L. Edwards, Michael P. Jennings, and Alastair G. McEwan. "A Periplasmic Thioredoxin-Like Protein Plays a Role in Defense against Oxidative Stress in Neisseria gonorrhoeae." Infection and Immunity 77, no. 11 (August 17, 2009): 4934–39. http://dx.doi.org/10.1128/iai.00714-09.

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ABSTRACT Thioredoxin-like proteins of the TlpA/ResE/CcmG subfamily are known to face the periplasm in gram-negative bacteria. Using the tlpA gene of Bradyrhizobium japonicum as a query, we identified a locus (NGO1923) in Neisseria gonorrhoeae that encodes a thioredoxin-like protein (NG_TlpA). Bioinformatics analysis indicated that the predicted NG_TlpA protein contained a cleavable signal peptide at the N terminus, and secondary structure analysis identified a thioredoxin fold with a helical insertion (∼25 residues), similar to that found in B. japonicum TlpA but absent in cytoplasmic thioredo

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Henderson, Brian, Peter Tabona, Stephen Poole, and Sean P. Nair. "Cloning and Expression of the Actinobacillus actinomycetemcomitans Thioredoxin (trx) Gene and Assessment of Cytokine Inhibitory Activity." Infection and Immunity 69, no. 1 (January 1, 2001): 154–58. http://dx.doi.org/10.1128/iai.69.1.154-158.2001.

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ABSTRACT Thioredoxin is a ubiquitous redox control and cell stress protein. Unexpectedly, in recent years, thioredoxins have been found to exhibit both cytokine and chemokine activities, and there is increasing evidence that this class of protein plays a role in the pathogenesis of inflammatory diseases. In spite of this evidence, it has been reported that the oral bacterium and periodontopathogen Actinobacillus actinomycetemcomitans secretes an immunosuppressive factor (termed suppressive factor 1 [SF1] [T. Kurita-Ochiai and K. Ochiai, Infect. Immun. 64:50–54, 1996]) whose N-terminal sequence

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Brown, Simone B., Raymond J. Turner, Rodney S. Roche, and Kenneth J. Stevenson. "Conformational analysis of thioredoxin using organoarsenical reagents as probes. A time-resolved fluorescence anisotropy and size exclusion chromatography study." Biochemistry and Cell Biology 67, no. 1 (January 1, 1989): 25–33. http://dx.doi.org/10.1139/o89-004.

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Reduced thioredoxin was subjected to chemical modification studies employing organoarsenical reagents specific for "spatially close" thiols. Modification was monitored by the loss in the free thiol content, by the percent incorporation of radiolabelled organoarsenical reagents, and by observing the changes in the amounts of the various thioredoxins by size exclusion chromatography. The rate of modification depends upon the polarity, rigidity, and size of the reagents. Small nonpolar organoarsenical reagents readily modified reduced thioredoxin, whereas polar and large reagents do not. Modifica

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Mihara, Shoko, Kazunori Sugiura, Keisuke Yoshida, and Toru Hisabori. "Thioredoxin targets are regulated in heterocysts of cyanobacterium Anabaena sp. PCC 7120 in a light-independent manner." Journal of Experimental Botany 71, no. 6 (December 21, 2019): 2018–27. http://dx.doi.org/10.1093/jxb/erz561.

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Abstract In the nitrogen-fixing cyanobacterium Anabaena sp. PCC 7120, glucose 6-phosphate dehydrogenase (G6PDH) plays an important role in producing the power for reducing nitrogenase under light conditions. Our previous study showed that thioredoxin suppresses G6PDH by reducing its activator protein OpcA, implying that G6PDH is inactivated under light conditions because thioredoxins are reduced by the photosynthetic electron transport system in cyanobacteria. To address how Anabaena sp. PCC 7120 maintains G6PDH activity even under light conditions when nitrogen fixation occurs, we investigate

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Kang, Zhenhui, Tong Qin, and Zhiping Zhao. "Thioredoxins and thioredoxin reductase in chloroplasts: A review." Gene 706 (July 2019): 32–42. http://dx.doi.org/10.1016/j.gene.2019.04.041.

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Ying, Sheng-Hua, Xiao-Hui Wang, and Ming-Guang Feng. "Characterization of a thioredoxin (BbTrx) from the entomopathogenic fungus Beauveria bassiana and its expression in response to thermal stress." Canadian Journal of Microbiology 56, no. 11 (November 2010): 934–42. http://dx.doi.org/10.1139/w10-081.

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A thioredoxin (BbTrx) was identified from the entomopathogenic fungus Beauveria bassiana . The cloned nucleotide sequence consisted of a 423-bp open reading frame encoding a 141-amino-acid thioredoxin, a 1011-bp 5′ region, and a 419-bp 3′ region. The deduced protein sequence of BbTrx, including a common 95-amino-acid conserved domain and a unique 46-amino-acid carboxy terminal region, was similar (≤38% identity) to that of other thioredoxins and phylogenetically closest to that from Neurospora crassa . In insulin solution containing dithiothreitol at 25 °C, recombinant BbTrx or a truncated for

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Keselman, Anna, Ranjan Nath Pulak, Keren Moyal, and Noah Isakov. "PICOT: A Multidomain Protein with Multiple Functions." ISRN Immunology 2011 (October 19, 2011): 1–7. http://dx.doi.org/10.5402/2011/426095.

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The PICOT protein possesses three highly conserved regions that include an aminoterminal thioredoxin-like homology domain and a tandem repeat of a carboxyterminal PICOT homology domain with an overall conformation that resembles a glutaredoxin homology domain. In contrast to the classical dithiol thioredoxins and glutaredoxins, PICOT possesses a single cysteine residue in each of its three domains and is therefore distinct from the classical thioredoxin and glutaredoxin redox enzymes. Recent studies demonstrated that PICOT is a prerequisite for mouse embryogenesis and participates in several i

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Muller, E. G. "A glutathione reductase mutant of yeast accumulates high levels of oxidized glutathione and requires thioredoxin for growth." Molecular Biology of the Cell 7, no. 11 (November 1996): 1805–13. http://dx.doi.org/10.1091/mbc.7.11.1805.

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A glutathione reductase null mutant of Saccharomyces cerevisiae was isolated in a synthetic lethal genetic screen for mutations which confer a requirement for thioredoxin. Yeast mutants that lack glutathione reductase (glr1 delta) accumulate high levels of oxidized glutathione and have a twofold increase in total glutathione. The disulfide form of glutathione increases 200-fold and represents 63% of the total glutathione in a glr1 delta mutant compared with only 6% in wild type. High levels of oxidized glutathione are also observed in a trx1 delta, trx2 delta double mutant (22% of total), in a

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Pérez-Pérez, María Esther, Alejandro Mata-Cabana, Ana María Sánchez-Riego, Marika Lindahl, and Francisco J. Florencio. "A Comprehensive Analysis of the Peroxiredoxin Reduction System in the Cyanobacterium Synechocystis sp. Strain PCC 6803 Reveals that All Five Peroxiredoxins Are Thioredoxin Dependent." Journal of Bacteriology 191, no. 24 (October 9, 2009): 7477–89. http://dx.doi.org/10.1128/jb.00831-09.

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ABSTRACT Cyanobacteria perform oxygenic photosynthesis, which gives rise to the continuous production of reactive oxygen species, such as superoxide anion radicals and hydrogen peroxide, particularly under unfavorable growth conditions. Peroxiredoxins, which are present in both chloroplasts and cyanobacteria, constitute a class of thiol-dependent peroxidases capable of reducing hydrogen peroxide as well as alkyl hydroperoxides. Chloroplast peroxiredoxins have been studied extensively and have been found to use a variety of endogenous electron donors, such as thioredoxins, glutaredoxins, or cyc

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Kunchithapautham, Kannan, B. Padmavathi, R. B. Narayanan, P. Kaliraj, and Alan L. Scott. "Thioredoxin from Brugia malayi: Defining a 16-Kilodalton Class of Thioredoxins from Nematodes." Infection and Immunity 71, no. 7 (July 2003): 4119–26. http://dx.doi.org/10.1128/iai.71.7.4119-4126.2003.

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ABSTRACT Thioredoxins are a family of small redox proteins that undergo NADPH-dependent reduction by thioredoxin reductase. This results in a supply of reducing equivalents that cells use in a wide variety of biological reactions, which include maintaining reduced forms of the enzymes important for protection against damage from high-energy oxygen radicals, the regulation of transcription factor activity, and the inhibition of apoptosis. Here we report on a new member of the thioredoxin family of proteins from the filarial nematode Brugia malayi, Bm-TRX-1, which defines a new subclass of 16-kD

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Buchko, Garry W., Stephen N. Hewitt, Wesley C. Van Voorhis, and Peter J. Myler. "Solution NMR structures of oxidized and reducedEhrlichia chaffeensisthioredoxin: NMR-invisible structure owing to backbone dynamics." Acta Crystallographica Section F Structural Biology Communications 74, no. 1 (January 1, 2018): 46–56. http://dx.doi.org/10.1107/s2053230x1701799x.

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Thioredoxins are small ubiquitous proteins that participate in a diverse variety of redox reactionsviathe reversible oxidation of two cysteine thiol groups in a structurally conserved active site. Here, the NMR solution structures of a reduced and oxidized thioredoxin fromEhrlichia chaffeensis(Ec-Trx, ECH_0218), the etiological agent responsible for human monocytic ehrlichiosis, are described. The overall topology of the calculated structures is similar in both redox states and is similar to those of other thioredoxins: a five-stranded, mixed β-sheet (β1–β3–β2–β4–β5) surrounded by four α-helic

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Bréhélin, Claire, Christophe Laloi, Aaron T. Setterdahl, David B. Knaff, and Yves Meyer. "Cytosolic, Mitochondrial Thioredoxins and Thioredoxin Reductases in Arabidopsis Thaliana." Photosynthesis Research 79, no. 3 (2004): 295–304. http://dx.doi.org/10.1023/b:pres.0000017165.55488.ca.

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Knaff, David B. "Oxidation-reduction properties of thioredoxins and thioredoxin-regulated enzymes." Physiologia Plantarum 110, no. 3 (July 18, 2008): 309–13. http://dx.doi.org/10.1111/j.1399-3054.2000.1100304.x.

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Knaff, David B. "Oxidation-reduction properties of thioredoxins and thioredoxin-regulated enzymes." Physiologia Plantarum 110, no. 3 (November 2000): 309–13. http://dx.doi.org/10.1034/j.1399-3054.2000.1100304.x.

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Holmgren, A. "Thioredoxin." Annual Review of Biochemistry 54, no. 1 (June 1985): 237–71. http://dx.doi.org/10.1146/annurev.bi.54.070185.001321.

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Yamawaki, Hideyuki, Judith Haendeler, and Bradford C. Berk. "Thioredoxin." Circulation Research 93, no. 11 (November 28, 2003): 1029–33. http://dx.doi.org/10.1161/01.res.0000102869.39150.23.

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HIROTA, KIICHI, HAJIME NAKAMURA, HIROSHI MASUTANI, and JUNJI YODOI. "Thioredoxin Superfamily and Thioredoxin-Inducing Agents." Annals of the New York Academy of Sciences 957, no. 1 (May 2002): 189–99. http://dx.doi.org/10.1111/j.1749-6632.2002.tb02916.x.

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BYKHOVSKI, ALEXEI, TATIANA GLOBUS, TATYANA KHROMOVA, BORIS GELMONT, and DWIGHT WOOLARD. "RESONANT TERAHERTZ SPECTROSCOPY OF BACTERIAL THIOREDOXIN IN WATER: SIMULATION AND EXPERIMENT." International Journal of High Speed Electronics and Systems 18, no. 01 (March 2008): 109–17. http://dx.doi.org/10.1142/s0129156408005187.

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The experimental and computational study of bacterial thioredoxin, an E. coli protein, at THz frequencies is presented. The absorption spectrum of the entire protein in water was studied numerically in the terahertz range (0.1 – 2 THz). In our work, the initial X-ray molecular structure of thioredoxin was optimized using the molecular dynamical (MD) simulations at room temperature and atmospheric pressure. The effect of a liquid content of a bacterial cell was taken into account explicitly via the simulation of water molecules using the TIP3P water model. Using atomic trajectories from the roo

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Hess, Natalia, Simon Richter, Michael Liebthal, Karl-Josef Dietz, and Angelika Mustroph. "The Phosphofructokinase Isoform AtPFK5 Is a Novel Target of Plastidic Thioredoxin-f-Dependent Redox Regulation." Antioxidants 10, no. 3 (March 7, 2021): 401. http://dx.doi.org/10.3390/antiox10030401.

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The chloroplast primary metabolism is of central importance for plant growth and performance. Therefore, it is tightly regulated in order to adequately respond to multiple environmental conditions. A major fluctuation that plants experience each day is the change between day and night, i.e., the change between assimilation and dissimilation. Among other mechanisms, thioredoxin-mediated redox regulation is an important component of the regulation of plastid-localized metabolic enzymes. While assimilatory processes such as the Calvin–Benson cycle are activated under illumination, i.e., under red

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AlOkda, Abdelrahman, and Jeremy M. Van Raamsdonk. "Evolutionarily Conserved Role of Thioredoxin Systems in Determining Longevity." Antioxidants 12, no. 4 (April 17, 2023): 944. http://dx.doi.org/10.3390/antiox12040944.

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Thioredoxin and thioredoxin reductase are evolutionarily conserved antioxidant enzymes that protect organisms from oxidative stress. These proteins also play roles in redox signaling and can act as a redox-independent cellular chaperone. In most organisms, there is a cytoplasmic and mitochondrial thioredoxin system. A number of studies have examined the role of thioredoxin and thioredoxin reductase in determining longevity. Disruption of either thioredoxin or thioredoxin reductase is sufficient to shorten lifespan in model organisms including yeast, worms, flies and mice, thereby indicating co

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KERN, Renée, Abderrahim MALKI, Arne HOLMGREN, and Gilbert RICHARME. "Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase." Biochemical Journal 371, no. 3 (May 1, 2003): 965–72. http://dx.doi.org/10.1042/bj20030093.

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Thioredoxin, thioredoxin reductase and NADPH form the thioredoxin system and are the major cellular protein disulphide reductase. We report here that Escherichia coli thioredoxin and thioredoxin reductase interact with unfolded and denatured proteins, in a manner similar to that of molecular chaperones that are involved in protein folding and protein renaturation after stress. Thioredoxin and/or thioredoxin reductase promote the functional folding of citrate synthase and α-glucosidase after urea denaturation. They also promote the functional folding of the bacterial galactose receptor, a prote

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Mallén-Ponce, Manuel J., María José Huertas, and Francisco J. Florencio. "Exploring the Diversity of the Thioredoxin Systems in Cyanobacteria." Antioxidants 11, no. 4 (March 28, 2022): 654. http://dx.doi.org/10.3390/antiox11040654.

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Cyanobacteria evolved the ability to perform oxygenic photosynthesis using light energy to reduce CO2 from electrons extracted from water and form nutrients. These organisms also developed light-dependent redox regulation through the Trx system, formed by thioredoxins (Trxs) and thioredoxin reductases (TRs). Trxs are thiol-disulfide oxidoreductases that serve as reducing substrates for target enzymes involved in numerous processes such as photosynthetic CO2 fixation and stress responses. We focus on the evolutionary diversity of Trx systems in cyanobacteria and discuss their phylogenetic relat

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Steinert, Peter, Karin Plank-Schumacher, Marisa Montemartini, Hans-Jürgen Hecht, and Leopold Flohé. "Permutation of the Active Site Motif of Tryparedoxin 2." Biological Chemistry 381, no. 3 (March 14, 2000): 211–19. http://dx.doi.org/10.1515/bc.2000.028.

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Abstract Tryparedoxins (TXN) are thioredoxinrelated proteins which, as trypanothione:peroxiredoxin oxidoreductases, constitute the trypanothionedependent antioxidant defense and may also serve as substrates for ribonucleotide reductase in trypanosomatids. The active site motif of TXN2, [40]WCPPCR[45], of Crithidia fasciculata was mutated by sitedirected mutagenesis and eight corresponding muteins were expressed in E. coli as terminally Histagged proteins, purified to homogeneity by nickel chelate chromatography, and characterized in terms of specific activity, specificity and, if possible, kin

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Benáková, Štěpánka, Blanka Holendová та Lydie Plecitá-Hlavatá. "Redox Homeostasis in Pancreatic β-Cells: From Development to Failure". Antioxidants 10, № 4 (27 березня 2021): 526. http://dx.doi.org/10.3390/antiox10040526.

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Redox status is a key determinant in the fate of β-cell. These cells are not primarily detoxifying and thus do not possess extensive antioxidant defense machinery. However, they show a wide range of redox regulating proteins, such as peroxiredoxins, thioredoxins or thioredoxin reductases, etc., being functionally compartmentalized within the cells. They keep fragile redox homeostasis and serve as messengers and amplifiers of redox signaling. β-cells require proper redox signaling already in cell ontogenesis during the development of mature β-cells from their progenitors. We bring details about

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Yang, Jie-Lin, Dong-Qiang Zhao, and Li-Ying Feng. "Thioredoxin, thioredoxin-interacting protein and digestive diseases." World Chinese Journal of Digestology 19, no. 18 (2011): 1926. http://dx.doi.org/10.11569/wcjd.v19.i18.1926.

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Arnér, Elias S. J., and Arne Holmgren. "Physiological functions of thioredoxin and thioredoxin reductase." European Journal of Biochemistry 267, no. 20 (October 2000): 6102–9. http://dx.doi.org/10.1046/j.1432-1327.2000.01701.x.

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Holmgren, Arne. "Redox regulation by thioredoxin and thioredoxin reductase." BioFactors 11, no. 1-2 (2000): 63–64. http://dx.doi.org/10.1002/biof.5520110117.

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Garrigós, Víctor, Cecilia Picazo, Emilia Matallana, and Agustín Aranda. "Wine Yeast Peroxiredoxin TSA1 Plays a Role in Growth, Stress Response and Trehalose Metabolism in Biomass Propagation." Microorganisms 8, no. 10 (October 6, 2020): 1537. http://dx.doi.org/10.3390/microorganisms8101537.

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Peroxiredoxins are a family of peroxide-degrading enzymes for challenging oxidative stress. They receive their reducing power from redox-controlling proteins called thioredoxins, and these, in turn, from thioredoxin reductase. The main cytosolic peroxiredoxin is Tsa1, a moonlighting protein that also acts as protein chaperone a redox switch controlling some metabolic events. Gene deletion of peroxiredoxins in wine yeasts indicate that TSA1, thioredoxins and thioredoxin reductase TRR1 are required for normal growth in medium with glucose and sucrose as carbon sources. TSA1 gene deletion also di

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