Gotowe bibliografie tematyczne / Thioredoxin

Gotowa bibliografia na temat „Thioredoxin”

Autor: Grafiati
Data publikacji: 4 czerwca 2021
Data aktualizacji: 25 maja 2024

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Artykuły w czasopismach na temat "Thioredoxin"

1

Langlotz, Petra, Wolfgang Wagner i Hartmut Follmann. "Green Algae (Scenedesmus obliquus) Contain Three Thioredoxins of Regular Size". Zeitschrift für Naturforschung C 41, nr 11-12 (1.12.1986): 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 I, II, and III. They bind specifically to antibodies against E. coli thioredoxin. Chloroplast-free mutant algae (strain C-2A′) lack thioredoxin f but contain all three regular thioredoxins. Species I and II have very similar amino acid composition and enzyme-stimulating activities. They are considered cytoplasmic thioredoxins which serve as hydrogen donors in algal deoxyribonucleotide biosynthesis. Thioredoxin III is of low activity towards all the presently tested enzymes and its physiological role remains unknown; its role as a glutaredoxin could be excluded. All non-photosynthetic plant cells analyzed so far (mutant algae, seeds, and roots) contain a set of three regular-size thioredoxins.
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2

Nikkanen, Lauri, Jouni Toivola, Manuel Guinea Diaz i Eevi Rintamäki. "Chloroplast thioredoxin systems: prospects for improving photosynthesis". Philosophical Transactions of the Royal Society B: Biological Sciences 372, nr 1730 (14.08.2017): 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 pathways, and in stress responses of plants. Of the two plant plastid thioredoxin systems, the ferredoxin-dependent system relays reducing equivalents from photosystem I via ferredoxin and ferredoxin-thioredoxin reductase (FTR) to chloroplast proteins, while NADPH-dependent thioredoxin reductase (NTRC) forms a complete thioredoxin system including both reductase and thioredoxin domains in a single polypeptide. Chloroplast thioredoxins transmit environmental light signals to biochemical reactions, which allows fine tuning of photosynthetic processes in response to changing environmental conditions. In this paper we focus on the recent reports on specificity and networking of chloroplast thioredoxin systems and evaluate the prospect of improving photosynthetic performance by modifying the activity of thiol regulators in plants.This article is part of the themed issue ‘Enhancing photosynthesis in crop plants: targets for improvement'.
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3

Nikkanen, Lauri, i Eevi Rintamäki. "Thioredoxin-dependent regulatory networks in chloroplasts under fluctuating light conditions". Philosophical Transactions of the Royal Society B: Biological Sciences 369, nr 1640 (19.04.2014): 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 systems, including two reductases dependent on ferredoxin and NADPH as reducing power, respectively, several types of thioredoxins, and the system to deliver thiol redox signals to the thylakoid membrane and lumen. Light controls the activity of chloroplast thioredoxin systems in two ways. First, light reactions activate the thioredoxin systems via donation of electrons to oxidized ferredoxin and NADP + , and second, light induces production of reactive oxygen species in chloroplasts which deactivate the components of the thiol redox network. The diversity and partial redundancy of chloroplast thioredoxin systems enable chloroplast metabolism to rapidly respond to ever-changing environmental conditions and to raise plant fitness in natural growth conditions.
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4

Cadet, F., i 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, nr 1 (1.07.1988): 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 thioredoxin concentrations. The use of immunological techniques shows that sedoheptulose-1,7-bisphosphatase and fructose-1,6-bisphosphatase are poorly related immunologically.
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5

SERRATO, Antonio J., Juan M. PÉREZ-RUIZ i Francisco J. CEJUDO. "Cloning of thioredoxin h reductase and characterization of the thioredoxin reductase–thioredoxin h system from wheat". Biochemical Journal 367, nr 2 (15.10.2002): 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 polypeptide deduced from this cDNA shows close similarity to NTRs from Arabidopsis, contains FAD- and NADPH-binding domains and a disulphide probably interacting with the disulphide at the active site of thioredoxin h. Wheat NTR was expressed in Escherichia coli as a His-tagged protein. The absorption spectrum of the purified recombinant protein is typical of flavoenzymes. Furthermore, it showed NADPH-dependent thioredoxin h reduction activity, thus confirming that the cDNA clone reported in the present study encodes wheat NTR. Using the His-tagged NTR and TRXhA (wheat thioredoxin h), we successfully reconstituted the wheat NTR—thioredoxin h system in vitro, as shown by the insulin reduction assay. A polyclonal antibody was raised against wheat NTR after immunization of rabbits with the purified His-tagged protein. This antibody efficiently detected a single polypeptide of the corresponding molecular mass in seed extracts and it allowed the analysis of the pattern of accumulation of NTR in different wheat organs and developmental stages. NTR shows a wide distribution in wheat, but, surprisingly, its accumulation in seeds is low, in contrast with the level of thioredoxins h.
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Langlotz, Petra, Wolfgang Wagner i Hartmut Follmann. "A Large Chloroplast Thioredoxin ƒ Found in Green Algae". Zeitschrift für Naturforschung C 41, nr 3 (1.03.1986): 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 cellulose, and Blue Sepharose. When tested in homologous enzyme systems, reduced thioredoxin ƒ strongly activated algal fructose-bis-phosphatase, but was inactive towards the cytoplasmic algal ribonucleotide reductase; NADP malate dehydrogenase was also stimulated. The protein is missing in extracts from a chloroplast-free mutant strain, C-2A′, but appears together with other chloroplast components upon illumination. Protein ƒ is therefore the main chloroplast thioredoxin of the green algae, probably corresponding to the smaller leaf chloroplast thioredoxins ƒ and m combined. Algal thioredoxin ƒ appears closely related, however, to the large thioredoxin found in a cyanobacterium, Anabaena sp.
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7

Bodenstein, Johanna, i Hartmut Follmann. "Characterization of Two Thioredoxins in Pig Heart Including a New Mitochondrial Protein". Zeitschrift für Naturforschung C 46, nr 3-4 (1.04.1991): 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, and c-thioredoxin possesses six cysteines. Heart extracts were also show n to contain a NADPH-specific thioredoxin reductase of the known mammalian type. A specific function or target enzyme of mt-thioredoxin has not as yet been established.
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8

Berndt, Carsten, Christopher Horst Lillig i 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, nr 3 (marzec 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 cells by the reduction of protein thiols. The reversible oxidation of Cys-Gly-Pro-Cys or Cys-Pro(Ser)-Tyr-Cys active site cysteine residues is used in reversible electron transport. Thioredoxins and glutaredoxins belong to corresponding systems consisting of NADPH, thioredoxin reductase, and thioredoxin or NADPH, glutathione reductase, glutathione, and glutaredoxin, respectively. Thioredoxin as well as glutaredoxin activities appear to be very important for the progression and severity of several cardiovascular disorders. These proteins function not only as antioxidants, they inhibit or activate apoptotic signaling molecules like apoptosis signal-regulating kinase 1 and Ras or transcription factors like NF-κB. Thioredoxin activity is regulated by the endogenous inhibitor thioredoxin-binding protein 2 (TBP-2), indicating an important role of the balance between thioredoxin and TBP-2 levels in cardiovascular diseases. In this review, we will summarize cardioprotective effects of endogenous thioredoxin and glutaredoxin systems as well as the high potential in clinical applications of exogenously applied thioredoxin or glutaredoxin or the induction of endogenous thioredoxin and glutaredoxin systems.
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Léveillard, Thierry, i 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 reducing power in the form of NADPH, the cofactor of thioredoxin reductase (TXNRD). While a complete extracellular TXN system is present in the blood in the form of circulating TXN1 and TXNDR1, the source of extracellular NADPH remains a mystery. In the absence of redox regenerating capacity, extracellular thioredoxins may rather be prooxidant agents. Rod-derived cone viability factor (RdCVF) is the product of intron retention of the nucleoredoxin-like 1 (NXNL1) gene, a secreted truncated thioredoxin-like protein. The other product encoded by the gene, RdCVFL, is an enzymatically active thioredoxin. This is a very singular example of positive feedback of a superthioredoxin system encoded by a single gene likely emerging during evolution from metabolic constraints on redox signaling.
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Langlotz, Petra, i Hartmut Follmann. "Notes: Formation of Large Thioredoxin f Accompanies Chloroplast Development in Scenedesmus obliquus". Zeitschrift für Naturforschung C 42, nr 11-12 (1.12.1987): 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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Rozprawy doktorskie na temat "Thioredoxin"

1

Paunescu, Karina. "DNA-Stabilität und Thioredoxin-Thioredoxin-Reduktase im Zellkern". [S.l.] : [s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=969680333.

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Osborne, Leisa Jane. "Characterisation of Thioredoxin Dimers: A Biochemical Study". Thesis, Griffith University, 2011. http://hdl.handle.net/10072/365531.

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In addition to the conserved active site cysteines that are responsible for the classical redox activity of thioredoxins (Trx’s), vertebrate Trx’s contain an additional three conserved cysteines at position 62, 69 and 73. These structural cysteines are known to be subjected to a variety of post translational modifications including dimerisation that are believed to contribute to the regulation and diversity of function of vertebrate Trx’s. Reports of the formation of “disulphide linked dimers” have been a long standing observation since the earliest studies on vertebrate Trx’s, however detailed studies on dimerisation have been limited in number and the extent of characterisation achieved. Despite the potential for a diversity of dimeric forms with different structural and functional properties there has been a common assumption arising from the literature (despite some evidence to the contrary) that all dimers so far described are much the same and all are redox inactive.
Thesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Biomolecular and Physical Science
Science, Environment, Engineering and Technology
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3

Missirlis, Fanis. "Functional characterization of novel thioredoxin reductase and thioredoxin peroxidase in Drosophila". Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2002. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp05/NQ65830.pdf.

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Shah, Fenil. "Thioredoxin and its Target Proteins: Thioredoxin Expression under Different Oxygen Conditions". Thesis, Griffith University, 2011. http://hdl.handle.net/10072/367670.

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Thioredoxin is an antioxidant protein that performs multiple functions in the intracellular and extracellular environment of cells. Thioredoxin is highly expressed in cancer cells, especially more metastatic and aggressive cancers. Previous studies have demonstrated a functional role for thioredoxin in cancer cell invasion, however little information is currently available regarding the role of thioredoxin in the invasive process. In order to perform these and other functions, thioredoxin interacts with several different protein partners. The primary aim of this project was to identify previously unknown binding partners for thioredoxin, particularly those involved in the cancer cell invasion process, on the cell surface of breast cancer cells. In order to identify the binding partners for thioredoxin, a kinetic trapping protocol was employed. Constructs that expressed a thioredoxin mutant wherein the second cysteine of the active site (Cys35) is changed to a serine, were utilized to perform trapping experiments. The trapping mutants remain covalently linked to the target protein (because they lack the second cysteine to resolve the mixed disulfide bond formed), allowing for purification of resulting thioredoxin–substrate complexes. One of the known protein partners for thioredoxin is Methionine Sulfoxide Reductase A (MsrA). Kinetic trapping experiments were performed to determine which of the four cysteine residues within the MsrA protein directly bound to thioredoxin. The experiments were performed using various MsrA cysteine mutants and determined that thioredoxin can bind to either the 3rd or 4th cysteine residue within the MsrA sequence. The kinetic trapping protocol was also used to attempt to identify previously unknown binding partners for thioredoxin on the surface of MDA-MB-231 breast cancer cells. Cell-surface trapping resulted in a single band visualized on anti-thioredoxin western blots, which indicates the recovery of a protein partner. However, the high number of cells used to get a positive result made it unrealistic to attempt even higher cell numbers which would be required in order to trap enough protein to identify the unknown protein partner.
Thesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Biomolecular and Physical Sciences
Science, Environment, Engineering and Technology
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Gregory, Mary Sarah-Jane, i n/a. "Thioredoxin and Oxidative Stress". Griffith University. School of Health Science, 2004. http://www4.gu.edu.au:8080/adt-root/public/adt-QGU20040301.082639.

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The experiments described in this thesis involve the expression and characterisation of recombinant truncated thioredoxin (tTrx) and the potential involvement that thioredoxin (Trx) has in the cellular responses to oxidative stress. Truncated Trx (80 amino acids) was expressed from a plasmid containing the ORF for tTrx that had been introduced into E.coli BL-21(DE3) cells. The protein was initially extracted using a combination of high concentrations of urea, high pH levels, and multiple sonification steps to remove the tTrx from inclusion bodies formed during expression. This procedure produced a stable solution of tTrx. Purification of tTrx from this protein solution required anion exchange chromatography followed by gel permeation in a HPLC system to obtain fully purified, recombinant tTrx which allowed further characterisation studies to be undertaken. An initial investigation into tTrx was performed to determine some basic physical, biochemical and functional aspects of this hitherto relatively undefined protein. Analysis by sedimentation equilibrium indicated that freshly prepared tTrx forms a single species with a molecular weight of 18.8kDa. This value indicates that recombinant tTrx naturally forms a dimer in solution that was shown to be non-covalent in nature and stable in solution. The capacity of tTrx to reduce protein disulphide bonds was determined using the insulin reduction assay. Results show that tTrx lacks this particular redox ability. The rate of oxidisation at 4 degrees C was analysed using free thiol determination, sedimentation equilibrium and SDS-PAGE patterning. Results indicated a steady rise in the degree of oxidation of tTrx over an eight day period. After six days the oxidated protein consistently displayed the presence of intramolecular disulphide bonds. Covalently-linked disulphide dimers and higher molecular weight oligomers were detectable after eight days oxidation. An investigation of the reducing capacity of the basic Trx system determined that fully oxidised tTrx was unable to act alone as a substrate for thioredoxin reductase (TR). However, when reduced Trx was added to the system, it appeared capable of acting as an electron donor to the oxidised tTrx in order to reduce disulphide groups. Recombinant tTrx was successfully radiolabelled with Trans 35S-methionine/cysteine for use in cell association studies. No evidence was found to indicate the presence of a receptor for tTrx on either MCF-7 or U-937 cells. Findings suggest that a low level of non-specific binding of tTrx to these cell lines rather than a classical ligand-binding mechanism occurs thus suggesting the absence of a cell surface receptor for tTrx. The role that Trx may play in the cellular responses to oxidative stress was also investigated. The chemical oxidants hydrogen peroxide (H2O2) and diamide were used to establish an in vitro model of oxidative stress for the choriocarcinoma cytotrophoblast cell line JEG-3. Cellular function was assessed in terms of membrane integrity, metabolic activity and the ability to synthesis new DNA following exposure to these oxidants. Results indicated that both agents were capable of causing cells to undergo oxidative stress without inducing immediate apoptosis or necrosis. Initially, JEG-3 cells exposed to 38μM or 75μM H2O2 or 100μM diamide were shown to display altered cell metabolism and DNA synthesis without loss to cell viability or membrane integrity. Cells were also shown to be capable of some short-term recovery but later lapsed into a more stressed state. Expression levels of Trx were studied to determine whether this type of chemical stress caused a change in intercellular protein levels. Both cELISA and western blotting results indicated that only cells exposed to 100μM diamide displayed any significant increase in Trx protein levels after 6 or 8hrs exposure to the oxidant. Further studies over a longer time-frame were also performed. These found that when JEG-3 cells were exposed to 18μM H2O2 or 200μM diamide over 12-48hrs, a positive correlation between increasing endogenous Trx protein levels and a decline in cell proliferation was observed. Cytotrophoblast cells, which are responsible for implantation and placentation, are susceptible to oxidative stress in vivo and their anti-oxidant capacity is fundamental to the establishment of pregnancy. The findings obtained during these studies suggest that Trx plays a role in this process.
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Gregory, Mary Sarah-Jane. "Thioredoxin and Oxidative Stress". Thesis, Griffith University, 2004. http://hdl.handle.net/10072/367183.

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The experiments described in this thesis involve the expression and characterisation of recombinant truncated thioredoxin (tTrx) and the potential involvement that thioredoxin (Trx) has in the cellular responses to oxidative stress. Truncated Trx (80 amino acids) was expressed from a plasmid containing the ORF for tTrx that had been introduced into E.coli BL-21(DE3) cells. The protein was initially extracted using a combination of high concentrations of urea, high pH levels, and multiple sonification steps to remove the tTrx from inclusion bodies formed during expression. This procedure produced a stable solution of tTrx. Purification of tTrx from this protein solution required anion exchange chromatography followed by gel permeation in a HPLC system to obtain fully purified, recombinant tTrx which allowed further characterisation studies to be undertaken. An initial investigation into tTrx was performed to determine some basic physical, biochemical and functional aspects of this hitherto relatively undefined protein. Analysis by sedimentation equilibrium indicated that freshly prepared tTrx forms a single species with a molecular weight of 18.8kDa. This value indicates that recombinant tTrx naturally forms a dimer in solution that was shown to be non-covalent in nature and stable in solution. The capacity of tTrx to reduce protein disulphide bonds was determined using the insulin reduction assay. Results show that tTrx lacks this particular redox ability. The rate of oxidisation at 4 degrees C was analysed using free thiol determination, sedimentation equilibrium and SDS-PAGE patterning. Results indicated a steady rise in the degree of oxidation of tTrx over an eight day period. After six days the oxidated protein consistently displayed the presence of intramolecular disulphide bonds. Covalently-linked disulphide dimers and higher molecular weight oligomers were detectable after eight days oxidation. An investigation of the reducing capacity of the basic Trx system determined that fully oxidised tTrx was unable to act alone as a substrate for thioredoxin reductase (TR). However, when reduced Trx was added to the system, it appeared capable of acting as an electron donor to the oxidised tTrx in order to reduce disulphide groups. Recombinant tTrx was successfully radiolabelled with Trans 35S-methionine/cysteine for use in cell association studies. No evidence was found to indicate the presence of a receptor for tTrx on either MCF-7 or U-937 cells. Findings suggest that a low level of non-specific binding of tTrx to these cell lines rather than a classical ligand-binding mechanism occurs thus suggesting the absence of a cell surface receptor for tTrx. The role that Trx may play in the cellular responses to oxidative stress was also investigated. The chemical oxidants hydrogen peroxide (H2O2) and diamide were used to establish an in vitro model of oxidative stress for the choriocarcinoma cytotrophoblast cell line JEG-3. Cellular function was assessed in terms of membrane integrity, metabolic activity and the ability to synthesis new DNA following exposure to these oxidants. Results indicated that both agents were capable of causing cells to undergo oxidative stress without inducing immediate apoptosis or necrosis. Initially, JEG-3 cells exposed to 38μM or 75μM H2O2 or 100μM diamide were shown to display altered cell metabolism and DNA synthesis without loss to cell viability or membrane integrity. Cells were also shown to be capable of some short-term recovery but later lapsed into a more stressed state. Expression levels of Trx were studied to determine whether this type of chemical stress caused a change in intercellular protein levels. Both cELISA and western blotting results indicated that only cells exposed to 100μM diamide displayed any significant increase in Trx protein levels after 6 or 8hrs exposure to the oxidant. Further studies over a longer time-frame were also performed. These found that when JEG-3 cells were exposed to 18μM H2O2 or 200μM diamide over 12-48hrs, a positive correlation between increasing endogenous Trx protein levels and a decline in cell proliferation was observed. Cytotrophoblast cells, which are responsible for implantation and placentation, are susceptible to oxidative stress in vivo and their anti-oxidant capacity is fundamental to the establishment of pregnancy. The findings obtained during these studies suggest that Trx plays a role in this process.
Thesis (Masters)
Master of Philosophy (MPhil)
School of Health Sciences
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7

Björkhem, Bergman Linda. "Thioredoxin reductase and selenium in carcinogenesis and multidrug resistance /". Stockholm, 2004. http://diss.kib.ki.se/2004/91-7349-954-4/.

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Zhong, Liangwei. "Selenium in mammalian thioredoxin reductase /". Stockholm, 2000. http://diss.kib.ki.se/2000/91-628-4243-9/.

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Callister, Matthew Eric James. "Thioredoxin and the inflammatory response". Thesis, Imperial College London, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.414905.

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Rozell, Björn. "Immunohistochemical studies of the thioredoxin system". Göteborg : Dept. of Histology, University of Göteborg, 1987. http://catalog.hathitrust.org/api/volumes/oclc/17242526.html.

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Książki na temat "Thioredoxin"

1

Joelson, Thorleif. Functional studies of bacteriophage T4 thioredoxin. Uppsala: Institutionen fo r molekyla rbiologi, 1988.

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2

Nikkola, Matti J. Structural and functional studies on glutaredoxin and thioredoxin. Uppsala: Swedish University of Agricultural Sciences, Dept. of Molecular Biology, 1991.

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3

Arne, Holmgren, i Karolinska Institute Nobel Conference on Thioredoxin and Glutaredoxin Systems: Structure and Function (1985 : Södergarn, Sweden), red. Thioredoxin and glutaredoxin systems: Structure and function. New York: Raven Press, 1986.

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4

Häberlein, Ingo. Charakterisierung der Thioredoxine und deren Zielsysteme in der Sojabohne (Glycine max). Gauting bei München: A.S. und Ch. C. Intemann, 1987.

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1942-, Sies H., i Packer Lester, red. Protein sensors and reactive oxygen species. San Diego, Calif: Academic Press, 2002.

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English, Shane. The cloning and characterization of the cDNA encoding mouse gamma-glutamyl cysteine synthetase and thioredoxin. Sudbury, Ont: Laurentian University, 2001.

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Lester, Packer, red. Biothiols. San Diego: Academic Press, 1995.

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service), ScienceDirect (Online, red. Thiol redox transitions in cell signaling: Cellular localization and signaling. San Diego, Calif: Elsevier, 2010.

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Thioredoxin and Glutaredoxin Systems. MDPI, 2019. http://dx.doi.org/10.3390/books978-3-03897-837-4.

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Holmgren, Arne. Thioredoxin and Glutaredoxin Systems: Structure and Function. Raven Pr, 1986.

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Części książek na temat "Thioredoxin"

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Didier, C., M. J. Richard, J. C. Beani i A. Favier. "Thioredoxin/Thioredoxin Reductase System". W Trace Elements in Man and Animals 10, 143. New York, NY: Springer US, 2002. http://dx.doi.org/10.1007/0-306-47466-2_36.

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Saccoccia, Fulvio, i Andrea Bellelli. "Thioredoxin Reductase". W Encyclopedia of Signaling Molecules, 5385–99. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101928.

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Hanschmann, Eva-Maria, i Carsten Berndt. "Thioredoxin (TXN)". W Encyclopedia of Signaling Molecules, 5377–85. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101939.

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Arnér, Elias S. J., i Arne Holmgren. "Thioredoxin System". W Encyclopedia of Cancer, 1–4. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27841-9_5777-3.

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Huang, Jin, i Liangwei Zhong. "Thioredoxin Reductase". W Advanced Topics in Science and Technology in China, 41–64. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-22236-8_3.

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Saccoccia, Fulvio, i Andrea Bellelli. "Thioredoxin Reductase". W Encyclopedia of Signaling Molecules, 1–15. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101928-1.

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Hanschmann, Eva-Maria, i Carsten Berndt. "Thioredoxin (TXN)". W Encyclopedia of Signaling Molecules, 1–9. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101939-1.

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Arnér, Elias S. J., i Arne Holmgren. "Thioredoxin System". W Encyclopedia of Cancer, 4508–11. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-46875-3_5777.

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Arnér, Elias S. J., i Arne Holmgren. "Thioredoxin System". W Encyclopedia of Cancer, 3670–71. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_5777.

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Schomburg, D., M. Salzmann i D. Stephan. "Thioredoxin reductase (NADPH)". W Enzyme Handbook 7, 267–71. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78521-4_53.

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Streszczenia konferencji na temat "Thioredoxin"

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Branković, Jovica, Vesna Milovanović, Zorica D. Petrović i Vladimir P. Petrović. "GALLIC ACID HYDRAZONES: ‘IN SILICO’ INHIBITION OF THIOREDOXIN REDUCTASE". W 1st INTERNATIONAL Conference on Chemo and BioInformatics. Institute for Information Technologies, University of Kragujevac, 2021. http://dx.doi.org/10.46793/iccbi21.320b.

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Gallic hydrazones, as gallic acid derivatives, are known as pharmacophores of numerous multipotent agents. Among them, antiproliferative activity is one of the most important. On the other hand, thioredoxin reductase (TrxR1) is a part of the thioredoxin system, one of the most important systems responsible for maintaining the redox equilibrium inside the cell. It is overexpressed in different forms of tumors. Bearing this in mind, TrxR1 is a valid target for the development of compounds with potential antiproliferative activity. For this purpose, eight gallic acid-based hydrazones are selected and examined in silico for their potential inhibitory activity towards TrxR1.
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Vitiello, Peter, i Elliot Bloom. "Hyperoxic Modification Of Thioredoxin-Dependent Pathways". W American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a5960.

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Vitiello, P., C. Aegerter, J. Hoffman, B. Mordhorst, A. Fairchild, B. Forred i T. E. Tipple. "Impairment of Thioredoxin 1 Disrupts Perinatal Alveolar Development". W American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a6043.

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Hu, H., L. Lu, E. Block i JM Patel. "Priming Donor Lungs with Thioredoxin Attenuates Allograft Rejection." W American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a5684.

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Vitiello, P., Y. Cao, C. Esslinger, C. Aegerter, K. Bruening, J. Hoffman, T. E. Tipple i B. Forred. "Hyperoxic Inhibition of Thioredoxin 1 Activity Disrupts Perinatal Alveologenesis". W American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a6394.

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Leaver, Susannah K., Gregory Quinlan, Timothy W. Evans i Anne Burke-Gaffney. "TNF ± MODIFIES THIOREDOXIN-INDUCED CYTOKINE RELEASE FROM HUMAN MONOCYTES". W American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a6150.

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Nikitjuka, Anna, i Raivis Žalubovskis. "Natural-like scaffolds targeting thioredoxin reductase for anticancer therapy". W 7th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/ecmc2021-11458.

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Ito, W., N. Kobayashi, M. Takeda, T. Tanigai, Y. Yamada, S. Ueki, H. Nakamura, H. Kayaba, J. Yodoi i J. Chihara. "Thioredoxin Reduces C-C Chemokine-Induced Chemotaxis of Human Eosinophils." W American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a1340.

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Rogozin, E. "Biotechnology for production of recombinant hybrid proteins from plants and microbes with antifungal activity". W 2nd International Scientific Conference "Plants and Microbes: the Future of Biotechnology". PLAMIC2020 Organizing committee, 2020. http://dx.doi.org/10.28983/plamic2020.206.

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The principle of obtaining recombinant antimicrobial polypeptides from plant and microbial origins as a part of chimeric proteins with thioredoxin by heterologous expression in a prokaryotic system is presented. The results obtained in terms of their antifungal activity in relation to plant pathogenic micromycetes allow us to consider these compounds as prototypes of some active substances of environmentally friendly biofungicides, as well as possible components of hybrid plant protection products against fungal diseases.
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Grandjean, Geoffrey, Geoffrey Bartholomeusz, John Kingston i Garth Powis. "Abstract 2188: A high throughput RNAi screen for regulators of thioredoxin in pancreatic cancer cells identifies components of TGFβ-signaling as inducers of thioredoxin expression". W Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2188.

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Raporty organizacyjne na temat "Thioredoxin"

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Lazo, John S. Novel Thioredoxin Inhibitors for Breast Cancer Therapy. Fort Belvoir, VA: Defense Technical Information Center, lipiec 2001. http://dx.doi.org/10.21236/ada396648.

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Lazo, John S. Novel Thioredoxin Inhibitors for Breast Cancer Therapy. Fort Belvoir, VA: Defense Technical Information Center, lipiec 2002. http://dx.doi.org/10.21236/ada409411.

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Porter, M. A., i F. C. Hartman. Thioredoxin binding site of phosphoribulokinase overlaps the catalytic site. [R]. Office of Scientific and Technical Information (OSTI), styczeń 1986. http://dx.doi.org/10.2172/5463659.

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Chuck, Steven L. The Non-Classical Secretion of Thioredoxin from Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, czerwiec 2002. http://dx.doi.org/10.21236/ada407677.

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Chuck, Steven L. The Non-Classical Secretion of Thioredoxin from Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, czerwiec 2004. http://dx.doi.org/10.21236/ada426431.

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Collier, Jackie, L. A Novel, Photosynthesis-Associated Thioredoxin-Like Gene: Final Technical Report. Office of Scientific and Technical Information (OSTI), wrzesień 2005. http://dx.doi.org/10.2172/850272.

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Chuck, Steven L. The Non-Classical Secretion of Thioredoxin from Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, czerwiec 2003. http://dx.doi.org/10.21236/ada425885.

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Cassidy, Pamela. Covalent Adducts Between Thioredoxin Reductase and Endogenous Electrophiles in Human Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, wrzesień 2005. http://dx.doi.org/10.21236/ada446694.

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Vargas Castro, José Livan, i MariCruz González García. Analysis of Regulatory Elements Related to Cytokinins and Interactions with Microorganisms in Promoters of Thioredoxins and Glutaredoxins. Fundación Avanza, maj 2024. http://dx.doi.org/10.60096/fundacionavanza/8642024.

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Análisis in silico de elementos reguladores de promotores de tiorredoxinas y glutarredoxinas para ver si estas proteínas pueden ser reguladas por citoquininas y elementos de interacción planta-microorganismos.
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Christopher, David A., i Avihai Danon. Plant Adaptation to Light Stress: Genetic Regulatory Mechanisms. United States Department of Agriculture, maj 2004. http://dx.doi.org/10.32747/2004.7586534.bard.

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Original Objectives: 1. Purify and biochemically characterize RB60 orthologs in higher plant chloroplasts; 2. Clone the gene(s) encoding plant RB60 orthologs and determine their structure and expression; 3. Manipulate the expression of RB60; 4. Assay the effects of altered RB60 expression on thylakoid biogenesis and photosynthetic function in plants exposed to different light conditions. In addition, we also examined the gene structure and expression of RB60 orthologs in the non-vascular plant, Physcomitrella patens and cloned the poly(A)-binding protein orthologue (43 kDa RB47-like protein). This protein is believed to a partner that interacts with RB60 to bind to the psbA5' UTR. Thus, to obtain a comprehensive view of RB60 function requires analysis of its biochemical partners such as RB43. Background & Achievements: High levels of sunlight reduce photosynthesis in plants by damaging the photo system II reaction center (PSII) subunits, such as D1 (encoded by the chloroplast tpsbAgene). When the rate of D1 synthesis is less than the rate of photo damage, photo inhibition occurs and plant growth is decreased. Plants use light-activated translation and enhanced psbAmRNA stability to maintain D1 synthesis and replace the photo damaged 01. Despite the importance to photosynthetic capacity, these mechanisms are poorly understood in plants. One intriguing model derived from the algal chloroplast system, Chlamydomonas, implicates the role of three proteins (RB60, RB47, RB38) that bind to the psbAmRNA 5' untranslated leader (5' UTR) in the light to activate translation or enhance mRNA stability. RB60 is the key enzyme, protein D1sulfide isomerase (Pill), that regulates the psbA-RN :Binding proteins (RB's) by way of light-mediated redox potentials generated by the photosystems. However, proteins with these functions have not been described from higher plants. We provided compelling evidence for the existence of RB60, RB47 and RB38 orthologs in the vascular plant, Arabidopsis. Using gel mobility shift, Rnase protection and UV-crosslinking assays, we have shown that a dithiol redox mechanism which resembles a Pill (RB60) activity regulates the interaction of 43- and 30-kDa proteins with a thermolabile stem-loop in the 5' UTR of the psbAmRNA from Arabidopsis. We discovered, in Arabidopsis, the PD1 gene family consists of II members that differ in polypeptide length from 361 to 566 amino acids, presence of signal peptides, KDEL motifs, and the number and positions of thioredoxin domains. PD1's catalyze the reversible formation an disomerization of disulfide bonds necessary for the proper folding, assembly, activity, and secretion of numerous enzymes and structural proteins. PD1's have also evolved novel cellular redox functions, as single enzymes and as subunits of protein complexes in organelles. We provide evidence that at least one Pill is localized to the chloroplast. We have used PDI-specific polyclonal and monoclonal antisera to characterize the PD1 (55 kDa) in the chloroplast that is unevenly distributed between the stroma and pellet (containing membranes, DNA, polysomes, starch), being three-fold more abundant in the pellet phase. PD1-55 levels increase with light intensity and it assembles into a high molecular weight complex of ~230 kDa as determined on native blue gels. In vitro translation of all 11 different Pill's followed by microsomal membrane processing reactions were used to differentiate among PD1's localized in the endoplasmic reticulum or other organelles. These results will provide.1e insights into redox regulatory mechanisms involved in adaptation of the photosynthetic apparatus to light stress. Elucidating the genetic mechanisms and factors regulating chloroplast photosynthetic genes is important for developing strategies to improve photosynthetic efficiency, crop productivity and adaptation to high light environments.
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