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Volumn 148, Issue 1, 2008, Pages 424-435

A novel type of thioredoxin dedicated to symbiosis in legumes

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA; EMBRYOPHYTA; MEDICAGO TRUNCATULA; NICOTIANA BENTHAMIANA; ORYZA SATIVA; POPULUS;

EID: 55549086871     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.108.123778     Document Type: Article
Times cited : (64)

References (45)
  • 1
    • 34247270164 scopus 로고    scopus 로고
    • Unique properties of NADP-thioredoxin reductase C in legumes
    • Alkhalfioui F, Renard M, Montrichard F (2007) Unique properties of NADP-thioredoxin reductase C in legumes. J Exp Bot 58: 969-978
    • (2007) J Exp Bot , vol.58 , pp. 969-978
    • Alkhalfioui, F.1    Renard, M.2    Montrichard, F.3
  • 2
    • 15944391748 scopus 로고    scopus 로고
    • A gene encoding a protein with a proline-rich domain (MtPPRD1), revealed by suppressive subtractive hybridization (SSH), is specifically expressed in the Medicago truncatula embryo axis during germination
    • Bouton S, Viau L, Lelievre E, Limami AM (2005) A gene encoding a protein with a proline-rich domain (MtPPRD1), revealed by suppressive subtractive hybridization (SSH), is specifically expressed in the Medicago truncatula embryo axis during germination. J Exp Bot 56: 825-832
    • (2005) J Exp Bot , vol.56 , pp. 825-832
    • Bouton, S.1    Viau, L.2    Lelievre, E.3    Limami, A.M.4
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantity of protein utilizing the principle of protein dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantity of protein utilizing the principle of protein dye binding. Anal Biochem 72: 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0035983856 scopus 로고    scopus 로고
    • The plastidic 2-cysteine peroxiredoxin is a target for a thioredoxin involved in the protection of the photosynthetic apparatus against oxidative damage
    • Broin M, Cuine S, Eymery F, Rey P (2002) The plastidic 2-cysteine peroxiredoxin is a target for a thioredoxin involved in the protection of the photosynthetic apparatus against oxidative damage. Plant Cell 14: 1417-1432
    • (2002) Plant Cell , vol.14 , pp. 1417-1432
    • Broin, M.1    Cuine, S.2    Eymery, F.3    Rey, P.4
  • 6
    • 0025923587 scopus 로고
    • Regulation of CO2 assimilation in oxygenic photosynthesis: The ferredoxin/thioredoxin system. Perspective on its discovery, present status, and future development
    • Buchanan BB (1991) Regulation of CO2 assimilation in oxygenic photosynthesis: the ferredoxin/thioredoxin system. Perspective on its discovery, present status, and future development. Arch Biochem Biophys 288: 1-9
    • (1991) Arch Biochem Biophys , vol.288 , pp. 1-9
    • Buchanan, B.B.1
  • 7
    • 20044367629 scopus 로고    scopus 로고
    • Redox regulation: A broadening horizon
    • Buchanan BB, Balmer Y (2005) Redox regulation: a broadening horizon. Annu Rev Plant Biol 56: 187-220
    • (2005) Annu Rev Plant Biol , vol.56 , pp. 187-220
    • Buchanan, B.B.1    Balmer, Y.2
  • 9
    • 0038157340 scopus 로고    scopus 로고
    • Differential expression and functional analysis of three calmodulin isoforms in germinating pea (Pisum sativum L.) seeds
    • Duval F, Renard M, Jaquinod M, Biou V, Montrichard F, Macherel D (2002) Differential expression and functional analysis of three calmodulin isoforms in germinating pea (Pisum sativum L.) seeds. Plant J 32: 481-493
    • (2002) Plant J , vol.32 , pp. 481-493
    • Duval, F.1    Renard, M.2    Jaquinod, M.3    Biou, V.4    Montrichard, F.5    Macherel, D.6
  • 10
    • 16544376129 scopus 로고    scopus 로고
    • Expression profiling in Medicago truncatula identifies more than 750 genes differentially expressed during nodulation, including many potential regulators of the symbiotic program
    • El Yahyaoui F, Kuster H, Ben Amor B, Hohnjec N, Puhler A, Becker A, Gouzy J, Vernie T, Gough C, Niebel A, et al (2004) Expression profiling in Medicago truncatula identifies more than 750 genes differentially expressed during nodulation, including many potential regulators of the symbiotic program. Plant Physiol 136: 3159-3176
    • (2004) Plant Physiol , vol.136 , pp. 3159-3176
    • El Yahyaoui, F.1    Kuster, H.2    Ben Amor, B.3    Hohnjec, N.4    Puhler, A.5    Becker, A.6    Gouzy, J.7    Vernie, T.8    Gough, C.9    Niebel, A.10
  • 11
    • 0024110181 scopus 로고
    • An NADP/ thioredoxin system in leaves: Purification and characterization of NADP-thioredoxin reductase and thioredoxin h from spinach
    • Florencio FJ, Yee BC, Johnson TC, Buchanan BB (1988) An NADP/ thioredoxin system in leaves: purification and characterization of NADP-thioredoxin reductase and thioredoxin h from spinach. Arch Biochem Biophys 266: 496-507
    • (1988) Arch Biochem Biophys , vol.266 , pp. 496-507
    • Florencio, F.J.1    Yee, B.C.2    Johnson, T.C.3    Buchanan, B.B.4
  • 13
    • 0346366724 scopus 로고    scopus 로고
    • Evidence for a subgroup of thioredoxin h that requires GSH/Grx for its reduction
    • Gelhaye E, Rouhier N, Jacquot JP (2003) Evidence for a subgroup of thioredoxin h that requires GSH/Grx for its reduction. FEBS Lett 555: 443-448
    • (2003) FEBS Lett , vol.555 , pp. 443-448
    • Gelhaye, E.1    Rouhier, N.2    Jacquot, J.P.3
  • 15
    • 0040799938 scopus 로고    scopus 로고
    • Oxidation-reduction properties of chloroplast thioredoxins, ferredoxin:thioredoxin reductase, and thioredoxin f-regulated enzymes
    • Hirasawa M, Schurmann P, Jacquot JP, Manieri W, Jacquot P, Keryer E, Hartman FC, Knaff DB (1999) Oxidation-reduction properties of chloroplast thioredoxins, ferredoxin:thioredoxin reductase, and thioredoxin f-regulated enzymes. Biochemistry 38: 5200-5205
    • (1999) Biochemistry , vol.38 , pp. 5200-5205
    • Hirasawa, M.1    Schurmann, P.2    Jacquot, J.P.3    Manieri, W.4    Jacquot, P.5    Keryer, E.6    Hartman, F.C.7    Knaff, D.B.8
  • 16
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Holmgren A (1979) Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J Biol Chem 254: 9627-9632
    • (1979) J Biol Chem , vol.254 , pp. 9627-9632
    • Holmgren, A.1
  • 20
    • 0028354036 scopus 로고
    • Arabidopsis thaliana NAPHP thioredoxin reductase. cDNA characterization and expression of the recombinant protein in Escherichia coli
    • Jacquot JP, Rivera-Madrid R, Marinho P, Kollarova M, Le Marechal P, Miginiac-Maslow M, Meyer Y (1994) Arabidopsis thaliana NAPHP thioredoxin reductase. cDNA characterization and expression of the recombinant protein in Escherichia coli. J Mol Biol 235: 1357-1363
    • (1994) J Mol Biol , vol.235 , pp. 1357-1363
    • Jacquot, J.P.1    Rivera-Madrid, R.2    Marinho, P.3    Kollarova, M.4    Le Marechal, P.5    Miginiac-Maslow, M.6    Meyer, Y.7
  • 21
    • 0023641348 scopus 로고
    • Thioredoxin and NADP-thioredoxin reductase from cultured carrot cells
    • Johnson TC, Cao RQ, Kung JE, Buchanan BB (1987) Thioredoxin and NADP-thioredoxin reductase from cultured carrot cells. Planta 171: 321-331
    • (1987) Planta , vol.171 , pp. 321-331
    • Johnson, T.C.1    Cao, R.Q.2    Kung, J.E.3    Buchanan, B.B.4
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 1642547085 scopus 로고    scopus 로고
    • The Arabidopsis cytosolic thioredoxin h5 gene induction by oxidative stress and its W-box-mediated response to pathogen elicitor
    • Laloi C, Mestres-Ortega D, Marco Y, Meyer Y, Reichheld JP (2004) The Arabidopsis cytosolic thioredoxin h5 gene induction by oxidative stress and its W-box-mediated response to pathogen elicitor. Plant Physiol 134: 1006-1016
    • (2004) Plant Physiol , vol.134 , pp. 1006-1016
    • Laloi, C.1    Mestres-Ortega, D.2    Marco, Y.3    Meyer, Y.4    Reichheld, J.P.5
  • 26
    • 33645000975 scopus 로고    scopus 로고
    • Induction of thioredoxin is required for nodule development to reduce reactive oxygen species levels in soybean roots
    • Lee MY, Shin KH, Kim YK, Suh JY, Gu YY, Kim MR, Hur YS, Son O, Kim JS, Song E, et al (2005) Induction of thioredoxin is required for nodule development to reduce reactive oxygen species levels in soybean roots. Plant Physiol 139: 1881-1889
    • (2005) Plant Physiol , vol.139 , pp. 1881-1889
    • Lee, M.Y.1    Shin, K.H.2    Kim, Y.K.3    Suh, J.Y.4    Gu, Y.Y.5    Kim, M.R.6    Hur, Y.S.7    Son, O.8    Kim, J.S.9    Song, E.10
  • 28
    • 0038393110 scopus 로고    scopus 로고
    • Characterization of thioredoxin y, a new type of thioredoxin identified in the genome of Chlamydomonas reinhardtii
    • Lemaire SD, Collin V, Keryer E, Quesada A, Miginiac-Maslow M (2003b) Characterization of thioredoxin y, a new type of thioredoxin identified in the genome of Chlamydomonas reinhardtii. FEBS Lett 543: 87-92
    • (2003) FEBS Lett , vol.543 , pp. 87-92
    • Lemaire, S.D.1    Collin, V.2    Keryer, E.3    Quesada, A.4    Miginiac-Maslow, M.5
  • 30
    • 0038663127 scopus 로고    scopus 로고
    • A novel family in Medicago truncatula consisting of more than 300 nodule-specific genes coding for small, secreted polypeptides with conserved cysteine motifs
    • Mergaert P, Nikovics K, Kelemen Z, Maunoury N, Vaubert D, Kondorosi A, Kondorosi E (2003) A novel family in Medicago truncatula consisting of more than 300 nodule-specific genes coding for small, secreted polypeptides with conserved cysteine motifs. Plant Physiol 132: 161-173
    • (2003) Plant Physiol , vol.132 , pp. 161-173
    • Mergaert, P.1    Nikovics, K.2    Kelemen, Z.3    Maunoury, N.4    Vaubert, D.5    Kondorosi, A.6    Kondorosi, E.7
  • 31
    • 0032735140 scopus 로고    scopus 로고
    • The Arabidopsis thaliana genome encodes at least four thioredoxins m and a new prokaryotic-like thioredoxin
    • Mestres-Ortega D, Meyer Y (1999) The Arabidopsis thaliana genome encodes at least four thioredoxins m and a new prokaryotic-like thioredoxin. Gene 240: 307-316
    • (1999) Gene , vol.240 , pp. 307-316
    • Mestres-Ortega, D.1    Meyer, Y.2
  • 32
    • 29944441650 scopus 로고    scopus 로고
    • Thioredoxins in Arabidopsis and other plants
    • Meyer Y, Reichheld JP, Vignols F (2005) Thioredoxins in Arabidopsis and other plants. Photosynth Res 86: 419-433
    • (2005) Photosynth Res , vol.86 , pp. 419-433
    • Meyer, Y.1    Reichheld, J.P.2    Vignols, F.3
  • 34
    • 0036119804 scopus 로고    scopus 로고
    • Classification of plant thioredoxins by sequence similarity and intron position
    • Meyer Y, Vignols F, Reichheld JP (2002) Classification of plant thioredoxins by sequence similarity and intron position. Methods Enzymol 347: 394-402
    • (2002) Methods Enzymol , vol.347 , pp. 394-402
    • Meyer, Y.1    Vignols, F.2    Reichheld, J.P.3
  • 35
    • 0038038334 scopus 로고    scopus 로고
    • Identification and differential expression of two thioredoxin h isoforms in germinating seeds from pea
    • Montrichard F, Renard M, Alkhalfioui F, Duval DF, Macherel D (2003) Identification and differential expression of two thioredoxin h isoforms in germinating seeds from pea. Plant Physiol 132: 1707-1715
    • (2003) Plant Physiol , vol.132 , pp. 1707-1715
    • Montrichard, F.1    Renard, M.2    Alkhalfioui, F.3    Duval, D.F.4    Macherel, D.5
  • 37
    • 33745816673 scopus 로고    scopus 로고
    • CITRX thioredoxin is a putative adaptor protein connecting Cf-9 and the ACIK1 protein kinase during the Cf-9/Avr9-induced defence response
    • Nekrasov V, Ludwig AA, Jones JDG (2006) CITRX thioredoxin is a putative adaptor protein connecting Cf-9 and the ACIK1 protein kinase during the Cf-9/Avr9-induced defence response. FEBS Lett 580: 4236-4241
    • (2006) FEBS Lett , vol.580 , pp. 4236-4241
    • Nekrasov, V.1    Ludwig, A.A.2    Jones, J.D.G.3
  • 38
    • 0036619752 scopus 로고    scopus 로고
    • The multigenic family of thioredoxin h in Arabidopsis thaliana: Specific expression and stress response
    • Reichheld JP, Mestres-Ortega D, Laloi C, Meyer Y (2002) The multigenic family of thioredoxin h in Arabidopsis thaliana: specific expression and stress response. Plant Physiol Biochem 40: 685-690
    • (2002) Plant Physiol Biochem , vol.40 , pp. 685-690
    • Reichheld, J.P.1    Mestres-Ortega, D.2    Laloi, C.3    Meyer, Y.4
  • 39
    • 2942535848 scopus 로고    scopus 로고
    • CITRX thioredoxin interacts with the tomato Cf-9 resistance protein and negatively regulates defence
    • Rivas S, Rougon-Cardoso A, Smoker M, Schauser L, Yoshioka H, Jones JD (2004) CITRX thioredoxin interacts with the tomato Cf-9 resistance protein and negatively regulates defence. EMBO J 22: 2156-2166
    • (2004) EMBO J , vol.22 , pp. 2156-2166
    • Rivas, S.1    Rougon-Cardoso, A.2    Smoker, M.3    Schauser, L.4    Yoshioka, H.5    Jones, J.D.6
  • 41
    • 0031666953 scopus 로고    scopus 로고
    • Identification of immunologically related proteins in sieve-tube exudate collected from monocotyledonous and dicotyledonous plants
    • Schobert C, Baker L, Szederkenyi J, Grossmann P, Komor E, Hayashi H, Chino M, Lucas WJ (1998) Identification of immunologically related proteins in sieve-tube exudate collected from monocotyledonous and dicotyledonous plants. Planta 206: 245-252
    • (1998) Planta , vol.206 , pp. 245-252
    • Schobert, C.1    Baker, L.2    Szederkenyi, J.3    Grossmann, P.4    Komor, E.5    Hayashi, H.6    Chino, M.7    Lucas, W.J.8
  • 42
    • 0029310608 scopus 로고
    • Chlamydomonas reinhardtii thioredoxins: Structure of the genes coding for the chloroplastic m and cytosolic h isoforms; expression in Escherichia coli of the recombinant proteins, purification and biochemical properties
    • Stein M, Jacquot JP, Jeannette E, Decottignies P, Hodges M, Lancelin JM, Mittard V, Schmitter JM, Miginiac-Maslow M (1995) Chlamydomonas reinhardtii thioredoxins: structure of the genes coding for the chloroplastic m and cytosolic h isoforms; expression in Escherichia coli of the recombinant proteins, purification and biochemical properties. Plant Mol Biol 28: 487-503
    • (1995) Plant Mol Biol , vol.28 , pp. 487-503
    • Stein, M.1    Jacquot, J.P.2    Jeannette, E.3    Decottignies, P.4    Hodges, M.5    Lancelin, J.M.6    Mittard, V.7    Schmitter, J.M.8    Miginiac-Maslow, M.9
  • 43
    • 34250661741 scopus 로고    scopus 로고
    • Thioredoxin h5 is required for victorin sensitivity mediated by a CC-NBS-LRR gene in Arabidopsis
    • Sweat TA, Wolpert TJ (2007) Thioredoxin h5 is required for victorin sensitivity mediated by a CC-NBS-LRR gene in Arabidopsis. Plant Cell 19: 673-687
    • (2007) Plant Cell , vol.19 , pp. 673-687
    • Sweat, T.A.1    Wolpert, T.J.2
  • 45
    • 26844472700 scopus 로고    scopus 로고
    • Dynamics of COPII vesicles and the Golgi apparatus in cultured Nicotiana tabacum BY-2 cells provides evidence for transient association of Golgi stacks with endoplasmic reticulum exit sites
    • Yang YD, Elamawi R, Bubeck J, Pepperkok R, Ritzenthaler C, Robinson DG (2005) Dynamics of COPII vesicles and the Golgi apparatus in cultured Nicotiana tabacum BY-2 cells provides evidence for transient association of Golgi stacks with endoplasmic reticulum exit sites. Plant Cell 17: 1513-1531
    • (2005) Plant Cell , vol.17 , pp. 1513-1531
    • Yang, Y.D.1    Elamawi, R.2    Bubeck, J.3    Pepperkok, R.4    Ritzenthaler, C.5    Robinson, D.G.6


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