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[PMID]:29298981
[Au] Autor:Díaz MG; Hernández-Verdeja T; Kremnev D; Crawford T; Dubreuil C; Strand Å
[Ad] Endereço:Umeå Plant Science Centre, Department of Plant Physiology, Umeå University, SE-901 87, Umeå, Sweden.
[Ti] Título:Redox regulation of PEP activity during seedling establishment in Arabidopsis thaliana.
[So] Source:Nat Commun;9(1):50, 2018 01 03.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Activation of the plastid-encoded RNA polymerase is tightly controlled and involves a network of phosphorylation and, as yet unidentified, thiol-mediated events. Here, we characterize PLASTID REDOX INSENSITIVE2, a redox-regulated protein required for full PEP-driven transcription. PRIN2 dimers can be reduced into the active monomeric form by thioredoxins through reduction of a disulfide bond. Exposure to light increases the ratio between the monomeric and dimeric forms of PRIN2. Complementation of prin2-2 with different PRIN2 protein variants demonstrates that the monomer is required for light-activated PEP-dependent transcription and that expression of the nuclear-encoded photosynthesis genes is linked to the activity of PEP. Activation of PEP during chloroplast development likely is the source of a retrograde signal that promotes nuclear LHCB expression. Thus, regulation of PRIN2 is the thiol-mediated mechanism required for full PEP activity, with PRIN2 monomerization via reduction by TRXs providing a mechanistic link between photosynthetic electron transport and activation of photosynthetic gene expression.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/enzimologia
Tiorredoxinas de Cloroplastos/metabolismo
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Plântulas/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Transporte de Elétrons
Fotossíntese
Plastídeos/metabolismo
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Chloroplast Thioredoxins); 0 (Intracellular Signaling Peptides and Proteins); 0 (PRIN2 protein, Arabidopsis); 0 (thioredoxin z, Arabidopsis)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180105
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02468-2


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[PMID]:28246333
[Au] Autor:Yoshida K; Hisabori T
[Ad] Endereço:Laboratory for Chemistry and Life Science, Tokyo Institute of Technology, Nagatsuta 4259-R1-8, Midori-ku, Yokohama 226-8503, Japan yoshida.k.ao@m.titech.ac.jp thisabor@res.titech.ac.jp.
[Ti] Título:Distinct electron transfer from ferredoxin-thioredoxin reductase to multiple thioredoxin isoforms in chloroplasts.
[So] Source:Biochem J;474(8):1347-1360, 2017 Apr 04.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Thiol-based redox regulation is considered to support light-responsive control of various chloroplast functions. The redox cascade via ferredoxin-thioredoxin reductase (FTR)/thioredoxin (Trx) has been recognized as a key to transmitting reducing power; however, genome sequencing has revealed that as many as five Trx subtypes encoded by a total of 10 nuclear genes are targeted to chloroplasts. Because each Trx isoform seems to have a distinct target selectivity, the electron distribution from FTR to multiple Trxs is thought to be the critical branch point for determining the consequence of chloroplast redox regulation. In the present study, we aimed to comprehensively characterize the kinetics of electron transfer from FTR to 10 Trx isoforms. We prepared the recombinant FTR protein from in the heterodimeric form containing the Fe-S cluster. By reconstituting the FTR/Trx system , we showed that FTR prepared here was enzymatically active and suitable for uncovering biochemical features of chloroplast redox regulation. A series of redox state determinations using the thiol-modifying reagent, 4-acetamido-4'-maleimidylstilbene-2,2'-disulfonate, indicated that all chloroplast Trx isoforms are commonly reduced by FTR; however, significantly different efficiencies were evident. These differences were apparently correlated with the distinct midpoint redox potentials among Trxs. Even when the experiments were performed under conditions of hypothetical stoichiometry of FTR and Trxs, a similar trend in distinguishable electron transfers was observed. These data highlight an aspect of highly organized circuits in the chloroplast redox regulation network.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Tiorredoxinas de Cloroplastos/metabolismo
Cloroplastos/metabolismo
Transporte de Elétrons
Proteínas com Ferro-Enxofre/metabolismo
Modelos Moleculares
Oxirredutases/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/enzimologia
Arabidopsis/metabolismo
Proteínas de Arabidopsis/química
Proteínas de Arabidopsis/genética
Biocatálise/efeitos dos fármacos
Domínio Catalítico
Tiorredoxinas de Cloroplastos/química
Tiorredoxinas de Cloroplastos/genética
Cloroplastos/enzimologia
Transporte de Elétrons/efeitos dos fármacos
Proteínas com Ferro-Enxofre/química
Proteínas com Ferro-Enxofre/genética
Oxirredução
Oxirredutases/química
Oxirredutases/genética
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Isoformas de Proteínas/química
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
Subunidades Proteicas/química
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Estilbenos/farmacologia
Reagentes de Sulfidrila/farmacologia
Ácidos Sulfônicos/farmacologia
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (4-acetamido-4'-maleimidylstilbene-2,2'-disulfonate); 0 (Arabidopsis Proteins); 0 (Chloroplast Thioredoxins); 0 (Iron-Sulfur Proteins); 0 (Peptide Fragments); 0 (Protein Isoforms); 0 (Protein Subunits); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); 0 (Stilbenes); 0 (Sulfhydryl Reagents); 0 (Sulfonic Acids); 0 (TRX m4 protein, Arabidopsis); EC 1.- (Oxidoreductases); EC 1.18.- (ferredoxin-thioredoxin reductase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170516
[Lr] Data última revisão:
170516
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170302
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20161089


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[PMID]:28131337
[Au] Autor:Gütle DD; Roret T; Hecker A; Reski R; Jacquot JP
[Ad] Endereço:Université de Lorraine, UMR 1136 Interactions Arbres Microorganismes, F-54500 Vandœuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres Microorganismes, F-54280 Champenoux, France; Plant Biotechnology, Faculty of Biology, University of Freiburg, Schänzlestr. 1, 79104 Freiburg, Germany; Speman
[Ti] Título:Dithiol disulphide exchange in redox regulation of chloroplast enzymes in response to evolutionary and structural constraints.
[So] Source:Plant Sci;255:1-11, 2017 Feb.
[Is] ISSN:1873-2259
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Redox regulation of chloroplast enzymes via disulphide reduction is believed to control the rates of CO fixation. The study of the thioredoxin reduction pathways and of various target enzymes lead to the following guidelines.
[Mh] Termos MeSH primário: Dióxido de Carbono/metabolismo
Tiorredoxinas de Cloroplastos/metabolismo
Cloroplastos/metabolismo
Dissulfetos/metabolismo
Fotossíntese/fisiologia
Plantas/metabolismo
Tolueno/análogos & derivados
[Mh] Termos MeSH secundário: Evolução Biológica
Cloroplastos/enzimologia
Oxirredução
Tolueno/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Chloroplast Thioredoxins); 0 (Disulfides); 142M471B3J (Carbon Dioxide); 3FPU23BG52 (Toluene); U89B11P7SC (dithiol)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170414
[Lr] Data última revisão:
170414
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170130
[St] Status:MEDLINE


  4 / 87 MEDLINE  
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[PMID]:27940305
[Au] Autor:Thormählen I; Zupok A; Rescher J; Leger J; Weissenberger S; Groysman J; Orwat A; Chatel-Innocenti G; Issakidis-Bourguet E; Armbruster U; Geigenberger P
[Ad] Endereço:Department Biologie I, Ludwig-Maximilians-Universität München, Grosshaderner Straße 2-4, 82152 Martinsried, Germany.
[Ti] Título:Thioredoxins Play a Crucial Role in Dynamic Acclimation of Photosynthesis in Fluctuating Light.
[So] Source:Mol Plant;10(1):168-182, 2017 Jan 09.
[Is] ISSN:1752-9867
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Sunlight represents the energy source for photosynthesis and plant growth. When growing in the field, plant photosynthesis has to manage strong fluctuations in light intensities. Regulation based on the thioredoxin (Trx) system is believed to ensure light-responsive control of photosynthetic reactions in the chloroplast. However, direct evidence for a role of this system in regulating dynamic acclimation of photosynthesis in fluctuating conditions is largely lacking. In this report we show that the ferredoxin-dependent Trxs m1 and m2 as well as the NADPH-dependent NTRC are both indispensable for photosynthetic acclimation in fluctuating light intensities. Arabidopsis mutants with combined deficiency in Trxs m1 and m2 show wild-type growth and photosynthesis under constant light condition, while photosynthetic parameters are strongly modified in rapidly alternating high and low light. Two independent trxm1m2 mutants show lower photosynthetic efficiency in high light, but surprisingly significantly higher photosynthetic efficiency in low light. Our data suggest that a main target of Trx m1 and m2 is the NADP-malate dehydrogenase involved in export of excess reductive power from the chloroplast. The decreased photosynthetic efficiency in the high-light peaks may thus be explained by a reduced capacity of the trxm1m2 mutants in the rapid light activation of this enzyme. In the ntrc mutant, dynamic responses of non-photochemical quenching of excitation energy and plastoquinone reduction state both were strongly attenuated in fluctuating light intensities, leading to a massive decrease in PSII quantum efficiency and a specific decrease in plant growth under these conditions. This is likely due to the decreased ability of the ntrc mutant to control the stromal NADP(H) redox poise. Taken together, our results indicate that NTRC is indispensable in ensuring the full range of dynamic responses of photosynthesis to optimize photosynthesis and maintain growth in fluctuating light, while Trxs m1 and m2 are indispensable for full activation of photosynthesis in the high-light periods but negatively affect photosynthetic efficiency in the low-light periods of fluctuating light.
[Mh] Termos MeSH primário: Aclimatação
Arabidopsis/fisiologia
Tiorredoxinas de Cloroplastos/fisiologia
Fotossíntese/fisiologia
[Mh] Termos MeSH secundário: Arabidopsis/genética
Arabidopsis/crescimento & desenvolvimento
Arabidopsis/efeitos da radiação
Proteínas de Arabidopsis/genética
Proteínas de Arabidopsis/metabolismo
Clorofila/metabolismo
Tiorredoxinas de Cloroplastos/genética
Tiorredoxinas de Cloroplastos/metabolismo
Luz
Malato Desidrogenase (NADP+)/metabolismo
Mutação
Oxirredução
Fotossíntese/efeitos da radiação
Tiorredoxina Dissulfeto Redutase/genética
Tiorredoxina Dissulfeto Redutase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Chloroplast Thioredoxins); 1406-65-1 (Chlorophyll); EC 1.1.1.82 (Malate Dehydrogenase (NADP+)); EC 1.8.1.9 (NTRC protein, Arabidopsis); EC 1.8.1.9 (Thioredoxin-Disulfide Reductase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161213
[St] Status:MEDLINE


  5 / 87 MEDLINE  
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[PMID]:26842981
[Au] Autor:Naranjo B; Diaz-Espejo A; Lindahl M; Cejudo FJ
[Ad] Endereço:Instituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla and CSIC, Avda Américo Vespucio, 49, 41092-Sevilla, Spain.
[Ti] Título:Type-f thioredoxins have a role in the short-term activation of carbon metabolism and their loss affects growth under short-day conditions in Arabidopsis thaliana.
[So] Source:J Exp Bot;67(6):1951-64, 2016 Mar.
[Is] ISSN:1460-2431
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Redox regulation plays a central role in the adaptation of chloroplast metabolism to light. Extensive biochemical analyses in vitro have identified f-type thioredoxins (Trxs) as the most important catalysts for light-dependent reduction and activation of the enzymes of the Calvin-Benson cycle. However, the precise function of type f Trxs in vivo and their impact on plant growth are still poorly known. To address this issue we have generated an Arabidopsis thaliana double knock-out mutant, termed trxf1f2, devoid of both f1 and f2 Trxs. Despite the essential function previously proposed for f-type Trxs, the visible phenotype of the trxf1f2 double mutant was virtually indistinguishable from the wild type when grown under a long-day photoperiod. However, the Trx f-deficient plants showed growth inhibition under a short-day photoperiod which was not rescued at high light intensity. The absence of f-type Trxs led to significantly lower photosynthetic electron transport rates and higher levels of non-photochemical energy quenching. Notably, the Trx f null mutant suffered from a shortage of photosystem I electron acceptors and delayed activation of carbon dioxide fixation following a dark-light transition. Two redox-regulated Calvin-Benson cycle enzymes, fructose 1,6-bisphosphatase (FBPase) and Rubisco activase, showed retarded and incomplete reduction in the double mutant upon illumination, compared with wild-type plants. These results show that the function of f-type Trxs in the rapid activation of carbon metabolism in response to light is not entirely compensated for by additional plastid redox systems, and suggest that these Trxs have an important role in the light adjustment of photosynthetic metabolism.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/crescimento & desenvolvimento
Arabidopsis/metabolismo
Carbono/metabolismo
Tiorredoxinas de Cloroplastos/metabolismo
Fotoperíodo
[Mh] Termos MeSH secundário: Arabidopsis/enzimologia
Arabidopsis/genética
Dióxido de Carbono/metabolismo
Transporte de Elétrons/efeitos da radiação
Regulação da Expressão Gênica de Plantas/efeitos da radiação
Cinética
Luz
Mutação/genética
Oxirredução/efeitos da radiação
Fotossíntese/efeitos da radiação
Complexo de Proteína do Fotossistema I/metabolismo
Complexo de Proteína do Fotossistema II/metabolismo
Desenvolvimento Vegetal/efeitos da radiação
Plantas Geneticamente Modificadas
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Chloroplast Thioredoxins); 0 (Photosystem I Protein Complex); 0 (Photosystem II Protein Complex); 0 (RNA, Messenger); 0 (Rca protein, Arabidopsis); 142M471B3J (Carbon Dioxide); 7440-44-0 (Carbon)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160205
[St] Status:MEDLINE
[do] DOI:10.1093/jxb/erw017


  6 / 87 MEDLINE  
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[PMID]:26773743
[Au] Autor:Okegawa Y; Motohashi K
[Ad] Endereço:Department of Bioresource and Environmental Sciences, Faculty of Life Sciences, Kyoto Sangyo University, Kamigamo Motoyama, Kita-ku, Kyoto 603-8555, Japan.
[Ti] Título:Expression of spinach ferredoxin-thioredoxin reductase using tandem T7 promoters and application of the purified protein for in vitro light-dependent thioredoxin-reduction system.
[So] Source:Protein Expr Purif;121:46-51, 2016 May.
[Is] ISSN:1096-0279
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Thioredoxins (Trxs) regulate the activity of target proteins in the chloroplast redox regulatory system. In vivo, a disulfide bond within Trxs is reduced by photochemically generated electrons via ferredoxin (Fd) and ferredoxin-thioredoxin reductase (FTR: EC 1.8.7.2). FTR is an αß-heterodimer, and the ß-subunit has a 4Fe-4S cluster that is indispensable for the electron transfer from Fd to Trxs. Reconstitution of the light-dependent Fd/Trx system, including FTR, is required for the biochemical characterization of the Trx-dependent reduction pathway in the chloroplasts. In this study, we generated functional FTR by simultaneously expressing FTR-α and -ß subunits under the control of tandem T7 promoters in Escherichia coli, and purifying the resulting FTR complex protein. The purified FTR complex exhibited spectroscopic absorption at 410 nm, indicating that it contained the Fe-S cluster. Modification of the expression system and simplification of the purification steps resulted in improved FTR complex yields compared to those obtained in previous studies. Furthermore, the light-dependent Trx-reduction system was reconstituted by using Fd, the purified FTR, and intact thylakoids.
[Mh] Termos MeSH primário: Tiorredoxinas de Cloroplastos/genética
Ferredoxinas/genética
Proteínas com Ferro-Enxofre/biossíntese
Oxirredutases/biossíntese
[Mh] Termos MeSH secundário: Tiorredoxinas de Cloroplastos/química
Tiorredoxinas de Cloroplastos/metabolismo
Cloroplastos/química
Cloroplastos/metabolismo
Transporte de Elétrons
Ferredoxinas/química
Ferredoxinas/metabolismo
Proteínas com Ferro-Enxofre/genética
Luz
Oxirredução
Oxirredutases/genética
Fotossíntese
Spinacia oleracea/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chloroplast Thioredoxins); 0 (Ferredoxins); 0 (Iron-Sulfur Proteins); EC 1.- (Oxidoreductases); EC 1.18.- (ferredoxin-thioredoxin reductase)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160117
[St] Status:MEDLINE


  7 / 87 MEDLINE  
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[PMID]:26468055
[Au] Autor:Okegawa Y; Motohashi K
[Ad] Endereço:Department of Bioresource and Environmental Sciences, Faculty of Life Sciences, Kyoto Sangyo University, Kamigamo Motoyama, Kita-ku, Kyoto, 603-8555, Japan.
[Ti] Título:Chloroplastic thioredoxin m functions as a major regulator of Calvin cycle enzymes during photosynthesis in vivo.
[So] Source:Plant J;84(5):900-13, 2015 Dec.
[Is] ISSN:1365-313X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Thioredoxins (Trxs) regulate the activity of various chloroplastic proteins in a light-dependent manner. Five types of Trxs function in different physiological processes in the chloroplast of Arabidopsis thaliana. Previous in vitro experiments have suggested that the f-type Trx (Trx f) is the main redox regulator of chloroplast enzymes, including Calvin cycle enzymes. To investigate the in vivo contribution of each Trx isoform to the redox regulatory system, we first quantified the protein concentration of each Trx isoform in the chloroplast stroma. The m-type Trx (Trx m), which consists of four isoforms, was the most abundant type. Next, we analyzed several Arabidopsis Trx-m-deficient mutants to elucidate the physiological role of Trx m in vivo. Deficiency of Trx m impaired plant growth and decreased the CO2 assimilation rate. We also determined the redox state of Trx target enzymes to examine their photo-reduction, which is essential for enzyme activation. In the Trx-m-deficient mutants, the reduction level of fructose-1,6-bisphosphatase and sedoheptulose-1,7-bisphosphatase was lower than that in the wild type. Inconsistently with the historical view, our in vivo study suggested that Trx m plays a more important role than Trx f in the activation of Calvin cycle enzymes.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/fisiologia
Arabidopsis/metabolismo
Tiorredoxinas de Cloroplastos/fisiologia
Cloroplastos/metabolismo
Fotossíntese
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Arabidopsis/genética
Arabidopsis/crescimento & desenvolvimento
Proteínas de Arabidopsis/metabolismo
Dióxido de Carbono/metabolismo
Tiorredoxinas de Cloroplastos/antagonistas & inibidores
Tiorredoxinas de Cloroplastos/metabolismo
Ativação Enzimática
Mutação
Oxirredução
Isoformas de Proteínas/metabolismo
Isoformas de Proteínas/fisiologia
Interferência de RNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Chloroplast Thioredoxins); 0 (Protein Isoforms); 142M471B3J (Carbon Dioxide); 8L70Q75FXE (Adenosine Triphosphate)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151016
[St] Status:MEDLINE
[do] DOI:10.1111/tpj.13049


  8 / 87 MEDLINE  
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[PMID]:25862497
[Au] Autor:Zhang M; Takano T; Liu S; Zhang X
[Ad] Endereço:Key Laboratory of Saline-alkali Vegetation Ecology Restoration in Oil Field (SAVER), Ministry of Education, Alkali Soil Natural Environmental Science Center (ASNESC), Northeast Forestry University, Harbin 150040, China.
[Ti] Título:Arabidopsis mitochondrial voltage-dependent anion channel 3 (AtVDAC3) protein interacts with thioredoxin m2.
[So] Source:FEBS Lett;589(11):1207-13, 2015 May 08.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Voltage-dependent anion channels (VDACs) are conserved mitochondrial outer membrane proteins. A yeast two-hybrid screen identified interaction between Arabidopsis VDAC3 and the chloroplast protein thioredoxin m2 (AtTrx m2). This was confirmed via pull-down assay. A bimolecular fluorescence complementation assay located the interaction in mitochondria. AtVDAC3 and AtTrx m2 transcripts were expressed in multiple tissues and up-regulated by abiotic stress. Under NaCl stress, AtVDAC3 overexpression inhibited growth and increased H2O2 accumulation, while AtTrx m2 overexpression conferred resistance to NaCl and reduced H2O2. Results indicate that both AtVDAC3 and AtTrx m2 are involved in ROS signaling and play opposite roles in NaCl stress response.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/enzimologia
Tiorredoxinas de Cloroplastos/metabolismo
Proteínas Mitocondriais/metabolismo
Transdução de Sinais/fisiologia
Estresse Fisiológico/fisiologia
Canais de Ânion Dependentes de Voltagem/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/genética
Proteínas de Arabidopsis/química
Proteínas de Arabidopsis/genética
Tiorredoxinas de Cloroplastos/química
Tiorredoxinas de Cloroplastos/genética
Peróxido de Hidrogênio/química
Peróxido de Hidrogênio/metabolismo
Proteínas Mitocondriais/química
Proteínas Mitocondriais/genética
Canais de Ânion Dependentes de Voltagem/química
Canais de Ânion Dependentes de Voltagem/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Chloroplast Thioredoxins); 0 (Mitochondrial Proteins); 0 (VDAC3 protein, Arabidopsis); 0 (Voltage-Dependent Anion Channels); BBX060AN9V (Hydrogen Peroxide)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:150508
[Lr] Data última revisão:
150508
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150412
[St] Status:MEDLINE


  9 / 87 MEDLINE  
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[PMID]:25202015
[Au] Autor:Morisse S; Michelet L; Bedhomme M; Marchand CH; Calvaresi M; Trost P; Fermani S; Zaffagnini M; Lemaire SD
[Ad] Endereço:From CNRS, UMR8226, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, Institut de Biologie Physico-Chimique, 75005 Paris, France, the Sorbonne Universités, Université Pierre et Marie Curie (UPMC) Universit́ Paris 06, UMR8226, Laboratoire de Biologie Moléculaire et Cellulaire des Euc
[Ti] Título:Thioredoxin-dependent redox regulation of chloroplastic phosphoglycerate kinase from Chlamydomonas reinhardtii.
[So] Source:J Biol Chem;289(43):30012-24, 2014 Oct 24.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In photosynthetic organisms, thioredoxin-dependent redox regulation is a well established mechanism involved in the control of a large number of cellular processes, including the Calvin-Benson cycle. Indeed, 4 of 11 enzymes of this cycle are activated in the light through dithiol/disulfide interchanges controlled by chloroplastic thioredoxin. Recently, several proteomics-based approaches suggested that not only four but all enzymes of the Calvin-Benson cycle may withstand redox regulation. Here, we characterized the redox features of the Calvin-Benson enzyme phosphoglycerate kinase (PGK1) from the eukaryotic green alga Chlamydomonas reinhardtii, and we show that C. reinhardtii PGK1 (CrPGK1) activity is inhibited by the formation of a single regulatory disulfide bond with a low midpoint redox potential (-335 mV at pH 7.9). CrPGK1 oxidation was found to affect the turnover number without altering the affinity for substrates, whereas the enzyme activation appeared to be specifically controlled by f-type thioredoxin. Using a combination of site-directed mutagenesis, thiol titration, mass spectrometry analyses, and three-dimensional modeling, the regulatory disulfide bond was shown to involve the not strictly conserved Cys(227) and Cys(361). Based on molecular mechanics calculation, the formation of the disulfide is proposed to impose structural constraints in the C-terminal domain of the enzyme that may lower its catalytic efficiency. It is therefore concluded that CrPGK1 might constitute an additional light-modulated Calvin-Benson cycle enzyme with a low activity in the dark and a TRX-dependent activation in the light. These results are also discussed from an evolutionary point of view.
[Mh] Termos MeSH primário: Chlamydomonas reinhardtii/enzimologia
Tiorredoxinas de Cloroplastos/metabolismo
Cloroplastos/enzimologia
Fosfoglicerato Quinase/metabolismo
[Mh] Termos MeSH secundário: Animais
Chlamydomonas reinhardtii/efeitos dos fármacos
Chlamydomonas reinhardtii/efeitos da radiação
Cloroplastos/efeitos dos fármacos
Cloroplastos/efeitos da radiação
Sequência Conservada
Cisteína/metabolismo
Dissulfetos/metabolismo
Ditiotreitol/farmacologia
Seres Humanos
Concentração de Íons de Hidrogênio
Cinética
Luz
Modelos Moleculares
Mutagênese Sítio-Dirigida
Proteínas Mutantes/metabolismo
Oxirredução/efeitos dos fármacos
Oxirredução/efeitos da radiação
Mapeamento de Peptídeos
Fosfoglicerato Quinase/química
Estrutura Terciária de Proteína
Análise de Sequência de Proteína
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
Sus scrofa
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chloroplast Thioredoxins); 0 (Disulfides); 0 (Mutant Proteins); EC 2.7.2.3 (Phosphoglycerate Kinase); K848JZ4886 (Cysteine); T8ID5YZU6Y (Dithiothreitol)
[Em] Mês de entrada:1502
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140910
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M114.597997


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[PMID]:25173453
[Au] Autor:Smiri M; Missaoui T
[Ad] Endereço:Department of Biotechnology, University of Carthage, Higher Institute of Sciences and Technology of Environment, Technopole of Borj Cedria, B.P. n° 1003, Hammam Lif 2050, Tunisia. Electronic address: smirimoez@yahoo.fr.
[Ti] Título:The role of ferredoxin:thioredoxin reductase/thioredoxin m in seed germination and the connection between this system and copper ion toxicity.
[So] Source:J Plant Physiol;171(17):1664-70, 2014 Nov 01.
[Is] ISSN:1618-1328
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Seed germination is highly sensitive to changes in the surrounding environment. This work examined the impact of imbibition with copper solution on the germination rate and behavior of some enzyme capacities involved in stress response. Chickpea (Cicer arietinum L.) seeds were germinated at 25°C in the dark for 7 days of imbibition with distilled water or an aqueous solution of chloride salt of 100 or 500µM CuCl2. The exposure of seeds to copper (Cu(2+)) induced changes in the antioxidant status. In Cu-treated seeds, the non-protein thiols (­SHNP) pool and ferredoxin:thioredoxin reductase (FTR) expression and activity increased. Cysteinyl sulfurs in the thioredoxin (Trx) function as ligands for metal ions. The accumulation of Cu(2+) inhibited seed germination and embryo growth. It appears that the FTR system mediates a novel form of redox signaling in plants under copper excess.
[Mh] Termos MeSH primário: Tiorredoxinas de Cloroplastos/metabolismo
Cicer/enzimologia
Cobre/toxicidade
Proteínas com Ferro-Enxofre/metabolismo
Oxirredutases/metabolismo
[Mh] Termos MeSH secundário: Antioxidantes/metabolismo
Biomassa
Cicer/efeitos dos fármacos
Cicer/genética
Cicer/crescimento & desenvolvimento
Cicer/fisiologia
Ferredoxinas/metabolismo
Germinação
Proteínas com Ferro-Enxofre/genética
Oxirredução
Oxirredutases/genética
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Sementes/efeitos dos fármacos
Sementes/enzimologia
Sementes/genética
Sementes/crescimento & desenvolvimento
Sementes/fisiologia
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antioxidants); 0 (Chloroplast Thioredoxins); 0 (Ferredoxins); 0 (Iron-Sulfur Proteins); 0 (Plant Proteins); 789U1901C5 (Copper); EC 1.- (Oxidoreductases); EC 1.18.- (ferredoxin-thioredoxin reductase); S2QG84156O (cupric chloride)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140901
[St] Status:MEDLINE



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