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Volumn 973, Issue , 2002, Pages 520-528

Redox control by dithiol-disulfide exchange in plants: II. The cytosolic and mitochondrial systems

Author keywords

Disulfide; Glutaredoxin; Glutathione; Peroxiredoxin; Thioredoxin

Indexed keywords

DISULFIDE; DITHIOL DERIVATIVE; FLAVOPROTEIN; GLUTAREDOXIN; GLUTATHIONE; GLUTATHIONE REDUCTASE; HYDROGEN PEROXIDE; PHOSPHATASE; PHOSPHOTRANSFERASE; PROTEIN; PROTEIN DERIVATIVE; PROTEIN GRX; PROTEIN TRX; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; THIOREDOXIN; THIOREDOXIN REDUCTASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 0036964026     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2002.tb04693.x     Document Type: Conference Paper
Times cited : (22)

References (41)
  • 1
    • 0036959783 scopus 로고    scopus 로고
    • Redox control by dithiol-disulfide exchange in plants. 1 The chloroplastic systems
    • This volume
    • JACQUOT, J.P., N. ROUHIER & E. GELHAYE. 2002. Redox control by dithiol-disulfide exchange in plants. 1. The chloroplastic systems. Ann. N.Y. Acad. Sci. This volume.
    • (2002) Ann. N.Y. Acad. Sci.
    • Jacquot, J.P.1    Rouhier, N.2    Gelhaye, E.3
  • 2
    • 0018786716 scopus 로고
    • Glutathione-dependent synthesis of deoxyribonucleotides. Characterization of the enzymatic mechanism of Escherichia coli glutaredoxin
    • HOLMGREN, A. 1979. Glutathione-dependent synthesis of deoxyribonucleotides. Characterization of the enzymatic mechanism of Escherichia coli glutaredoxin. J. Biol. Chem. 254: 3672-3678.
    • (1979) J. Biol. Chem. , vol.254 , pp. 3672-3678
    • Holmgren, A.1
  • 3
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • HOLMGREN, A. 1989. Thioredoxin and glutaredoxin systems. J. Biol. Chem. 264: 13963-13966.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 4
    • 0033767925 scopus 로고    scopus 로고
    • Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress
    • CARMEL-HAREL, O. & G. STORZ. 2000. Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress. Annu. Rev. Microbiol. 54: 439-461.
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 439-461
    • Carmel-Harel, O.1    Storz, G.2
  • 5
    • 0034534190 scopus 로고    scopus 로고
    • Molecular views of redox regulation: Three-dimensional structures of redox regulatory proteins and protein complexes
    • QIN, J., Y. YANG, A. VELYVIS & A. GRONENBORN. 2000. Molecular views of redox regulation: three-dimensional structures of redox regulatory proteins and protein complexes. Antioxid. Redox Signal. 2: 827-840.
    • (2000) Antioxid. Redox Signal. , vol.2 , pp. 827-840
    • Qin, J.1    Yang, Y.2    Velyvis, A.3    Gronenborn, A.4
  • 6
    • 0028354036 scopus 로고
    • Arabidopsis thaliana NADPH thioredoxin reductase. cDNA characterization and expression of the recombinant protein in Escherichia coli
    • JACQUOT, J.P., R. RIVERA-MADRID, P. MARINHO, et al. 1994. Arabidopsis thaliana NADPH 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
  • 7
    • 0035923520 scopus 로고    scopus 로고
    • Identification and characterization of a mitochondrial thioredoxin system in plants
    • LALOI, C., N. RAYAPURAM, Y. CHARTIER, et al. 2001. Identification and characterization of a mitochondrial thioredoxin system in plants. Proc. Natl. Acad. Sci. USA 98: 14144-14149.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14144-14149
    • Laloi, C.1    Rayapuram, N.2    Chartier, Y.3
  • 8
    • 0030596062 scopus 로고    scopus 로고
    • Crystal structure of Arabidopsis thaliana NADPH dependent thioredoxin reductase at 2.5 Å resolution
    • DAI, S., M. SAARINEN, S. RAMASWAMY, et al. 1996. Crystal structure of Arabidopsis thaliana NADPH dependent thioredoxin reductase at 2.5 Å resolution. J. Mol. Biol. 264: 1044-1057.
    • (1996) J. Mol. Biol. , vol.264 , pp. 1044-1057
    • Dai, S.1    Saarinen, M.2    Ramaswamy, S.3
  • 9
    • 0031026291 scopus 로고    scopus 로고
    • NMR solution structure of an oxidised thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii
    • MITTARD, V., M.J. BLACKLEDGE, M. STEIN, et al. 1997. NMR solution structure of an oxidised thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii. Eur. J. Biochem. 243: 374-383.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 374-383
    • Mittard, V.1    Blackledge, M.J.2    Stein, M.3
  • 10
    • 0035476417 scopus 로고    scopus 로고
    • Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism
    • MENCHISE, V., C. CORBIER, C. DIDIERJEAN, et al. 2001. Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism. Biochem. J. 359: 65-75.
    • (2001) Biochem. J. , vol.359 , pp. 65-75
    • Menchise, V.1    Corbier, C.2    Didierjean, C.3
  • 11
    • 0033951364 scopus 로고    scopus 로고
    • pH and temperature dependent aggregation of thioredoxin
    • LEMAIRE, S., J. RICHARDSON, A. GOYER, et al. 2000. pH and temperature dependent aggregation of thioredoxin. Biochim. Biophys. Acta 1476: 311-323.
    • (2000) Biochim. Biophys. Acta , vol.1476 , pp. 311-323
    • Lemaire, S.1    Richardson, J.2    Goyer, A.3
  • 13
    • 0034641693 scopus 로고    scopus 로고
    • Cold and heat dependent unfolding of thioredoxin h from Chlamydomonas reinhardtii involve different mechanisms: Spectroscopic and calorimetcic studies
    • RICHARDSON, J.M., S. LEMAIRE, J.P. JACQUOT & G.I. MAKHATADZE. 2000. Cold and heat dependent unfolding of thioredoxin h from Chlamydomonas reinhardtii involve different mechanisms: spectroscopic and calorimetcic studies. Biochemistry 39: 11154-11162.
    • (2000) Biochemistry , vol.39 , pp. 11154-11162
    • Richardson, J.M.1    Lemaire, S.2    Jacquot, J.P.3    Makhatadze, G.I.4
  • 14
    • 0033538442 scopus 로고    scopus 로고
    • In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family
    • VERDOUCQ, L., J.P. JACQUOT, F. VIGNOLS, et al. 1999. In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family. J. Biol. Chem. 274: 19714-19722.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19714-19722
    • Verdoucq, L.1    Jacquot, J.P.2    Vignols, F.3
  • 15
    • 0036157915 scopus 로고    scopus 로고
    • Isolation and characterization of a thioredoxin dependent peroxidase from Chlamydomonas reinhardtii
    • GOYER, A., C. HALESKAS, M. MIGINIAC-MASLOW, et al. 2002. Isolation and characterization of a thioredoxin dependent peroxidase from Chlamydomonas reinhardtii. Eur. J. Biochem. 269: 1-11.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1-11
    • Goyer, A.1    Haleskas, C.2    Miginiac-Maslow, M.3
  • 16
    • 0035202123 scopus 로고    scopus 로고
    • Isolation and characterization of a new peroxiredoxin from poplar sieve tubes that uses either glutaredoxin or thioredoxin as a proton donor
    • ROUHIER, N., E. GELHAYE, P.E. SAUTIERE, et al. 2001. Isolation and characterization of a new peroxiredoxin from poplar sieve tubes that uses either glutaredoxin or thioredoxin as a proton donor. Plant Physiol. 127: 1299-1309.
    • (2001) Plant Physiol. , vol.127 , pp. 1299-1309
    • Rouhier, N.1    Gelhaye, E.2    Sautiere, P.E.3
  • 17
    • 0033796101 scopus 로고    scopus 로고
    • The role of the redox protein thioredoxin in cell growth and cancer
    • POWIS, G., D. MUSTACICH & A. COON. 2000. The role of the redox protein thioredoxin in cell growth and cancer. Free Radical Biol. Med. 29: 312-322.
    • (2000) Free Radical Biol. Med. , vol.29 , pp. 312-322
    • Powis, G.1    Mustacich, D.2    Coon, A.3
  • 18
    • 0032514922 scopus 로고    scopus 로고
    • Regulation of the cyanide-resistant alternative oxidase of plant mitochondria. Identification of the cysteine residue involved in alpha-keto acid stimulation and intersubunit disulfide bond formation
    • RHOADS, D.M., A.L. UMBACH, C.R. SWEET, et al. 1998. Regulation of the cyanide-resistant alternative oxidase of plant mitochondria, identification of the cysteine residue involved in alpha-keto acid stimulation and intersubunit disulfide bond formation. J. Biol. Chem. 273: 30750-30756.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30750-30756
    • Rhoads, D.M.1    Umbach, A.L.2    Sweet, C.R.3
  • 19
    • 0035854785 scopus 로고    scopus 로고
    • Cloning and expression of a novel human glutaredoxin (Grx2) with mitochondrial and nuclear isoforms
    • LUNDBERG, M, C. JOHANSSON, J. CHANDRA, et al. 2001. Cloning and expression of a novel human glutaredoxin (Grx2) with mitochondrial and nuclear isoforms. J. Biol. Chem. 276: 26269-26275.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26269-26275
    • Lundberg, M.1    Johansson, C.2    Chandra, J.3
  • 20
    • 0025993780 scopus 로고
    • A putative glutathione-binding site in T4 glutaredoxin investigated by site-directed mutagenesis
    • NIKKOLA, M., F.K. GLEASON, M. SAARINEN, et al. 1991. A putative glutathione-binding site in T4 glutaredoxin investigated by site-directed mutagenesis. J. Biol. Chem. 266: 16105-16112.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16105-16112
    • Nikkola, M.1    Gleason, F.K.2    Saarinen, M.3
  • 21
    • 0021456845 scopus 로고
    • Conformational and functional similarities between glutaredoxin and thioredoxins
    • EKLUND, H., C. CAMBILLAU, B.M. SJOBERG, et al. 1984. Conformational and functional similarities between glutaredoxin and thioredoxins. EMBO J. 3: 1443-1449.
    • (1984) EMBO J. , vol.3 , pp. 1443-1449
    • Eklund, H.1    Cambillau, C.2    Sjoberg, B.M.3
  • 22
    • 0037196446 scopus 로고    scopus 로고
    • Exploring the active site of plant glutaredoxin by site-directed mutagenesis
    • ROUHIER, N., E. GELHAYE & J.P. JACQUOT. 2002. Exploring the active site of plant glutaredoxin by site-directed mutagenesis. FEBS Lett. 511: 145-149.
    • (2002) FEBS Lett. , vol.511 , pp. 145-149
    • Rouhier, N.1    Gelhaye, E.2    Jacquot, J.P.3
  • 23
    • 0030695902 scopus 로고    scopus 로고
    • Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria
    • ASLUND, F., K.D. BERNDT & A. HOLMGREN. 1997. Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria. J. Biol. Chem. 272: 30780-30786.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30780-30786
    • Aslund, F.1    Berndt, K.D.2    Holmgren, A.3
  • 24
    • 0028153876 scopus 로고
    • Cloning and sequence analysis of a cDNA encoding rice glutaredoxin
    • MINAKUCHI, K., T. YABUSHITA, T. MASUMARA, et al. 1994. Cloning and sequence analysis of a cDNA encoding rice glutaredoxin. FEBS Lett. 337: 157-160.
    • (1994) FEBS Lett. , vol.337 , pp. 157-160
    • Minakuchi, K.1    Yabushita, T.2    Masumara, T.3
  • 25
    • 1842376834 scopus 로고    scopus 로고
    • Cloning of the cDNA for glutaredoxin, an abundant sieve-tube exudate protein from Ricinus communis L. and characterisation of the glutathione-dependent thiol-reduction system in sieve tubes
    • SZEDERKENYI, J., E. KOMOR & C. SCHOBERT. 1997. Cloning of the cDNA for glutaredoxin, an abundant sieve-tube exudate protein from Ricinus communis L. and characterisation of the glutathione-dependent thiol-reduction system in sieve tubes. Planta 202: 349-356.
    • (1997) Planta , vol.202 , pp. 349-356
    • Szederkenyi, J.1    Komor, E.2    Schobert, C.3
  • 26
    • 0036511657 scopus 로고    scopus 로고
    • Enhancement of poplar glutaredoxin expression by optimization of the cDNA sequence
    • ROUHIER, N., E. GELHAYE, P.E. SAUTIERE & J.P. JACQUOT. 2002. Enhancement of poplar glutaredoxin expression by optimization of the cDNA sequence. Prot. Exp. Purif. 24: 234-241.
    • (2002) Prot. Exp. Purif. , vol.24 , pp. 234-241
    • Rouhier, N.1    Gelhaye, E.2    Sautiere, P.E.3    Jacquot, J.P.4
  • 27
    • 0037134534 scopus 로고    scopus 로고
    • Glutaredoxin dependent peroxiredoxin from poplar: Protein-protein interaction and catalytic mechanism
    • ROUHIER, N., E. GELHAYE & J.P. JACQUOT. 2002. Glutaredoxin dependent peroxiredoxin from poplar: protein-protein interaction and catalytic mechanism. J. Biol. Chem. 277: 13609-13614.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13609-13614
    • Rouhier, N.1    Gelhaye, E.2    Jacquot, J.P.3
  • 28
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: An overview
    • HALLIWELL, B. & J.M. GUTTERIDGE. 1990. Role of free radicals and catalytic metal ions in human disease: an overview. Methods Enzymol. 186: 1-85.
    • (1990) Methods Enzymol. , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.2
  • 29
    • 0030851732 scopus 로고    scopus 로고
    • Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro
    • DAVIS, D.A., F.M. NEWCOMB, D.W. STARKE, et al. 1997. Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro. J. Biol. Chem. 272: 25935-25940.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25935-25940
    • Davis, D.A.1    Newcomb, F.M.2    Starke, D.W.3
  • 30
    • 0032543374 scopus 로고    scopus 로고
    • Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: Catalysis by glutaredoxin
    • LIND, C., R. GERDES, I. SCHUPPE-KOISTINEN & I.A. COTGREAVE. 1998. Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: catalysis by glutaredoxin. Biochem. Biophys. Res. Commun. 247: 481-486.
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 481-486
    • Lind, C.1    Gerdes, R.2    Schuppe-Koistinen, I.3    Cotgreave, I.A.4
  • 31
    • 0035930608 scopus 로고    scopus 로고
    • Reversible glutathionylation regulates actin polymerization in A431 cells
    • WANG, J., E.S. BOJA, W. TAN, et al. 2001. Reversible glutathionylation regulates actin polymerization in A431 cells. J. Biol. Chem. 276: 47763-47766.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47763-47766
    • Wang, J.1    Boja, E.S.2    Tan, W.3
  • 32
    • 0031973308 scopus 로고    scopus 로고
    • Thioltransferase (glutaredoxin) reactivates the DNA-binding activity of oxidation-inactivated nuclear factor I
    • BANDYOPADHYAY, S., D.W. STARKE, J.J. MIEYAL & R.M. GRONOSTAJSKI. 1998. Thioltransferase (glutaredoxin) reactivates the DNA-binding activity of oxidation-inactivated nuclear factor I. J. Biol. Chem. 273: 392-397.
    • (1998) J. Biol. Chem. , vol.273 , pp. 392-397
    • Bandyopadhyay, S.1    Starke, D.W.2    Mieyal, J.J.3    Gronostajski, R.M.4
  • 33
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • ZHENG, M., F. ASLUND & G. STORZ. 1998. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279: 1718-1721.
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3
  • 34
    • 0035847101 scopus 로고    scopus 로고
    • Glutaredoxin protects cerebellar granule neurons from dopamine-induced apoptosis by activating NF-kappa B via Ref-1
    • DAILY, D., A. VLAMIS-GARDIKAS, D. OFFEN, et al. 2001. Glutaredoxin protects cerebellar granule neurons from dopamine-induced apoptosis by activating NF-kappa B via Ref-1. J. Biol. Chem. 276: 1335-1344.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1335-1344
    • Daily, D.1    Vlamis-Gardikas, A.2    Offen, D.3
  • 35
    • 0035877650 scopus 로고    scopus 로고
    • Glutaredoxin protects cerebellar granule neurons from dopamine-induced apoptosis by dual activation of the rasphosphoinositide 3-kinase and jun n-terminal kinase pathways
    • DAILY, D., A. VLAMIS-GARDIKAS, D. OFFEN, et al. 2001. Glutaredoxin protects cerebellar granule neurons from dopamine-induced apoptosis by dual activation of the rasphosphoinositide 3-kinase and jun n-terminal kinase pathways. J. Biol. Chem. 276: 21618-21626.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21618-21626
    • Daily, D.1    Vlamis-Gardikas, A.2    Offen, D.3
  • 36
    • 0028139014 scopus 로고
    • The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase
    • BJORNSTEDT, M., J. XUE, W. HUANG, et al. 1994. The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase. J. Biol. Chem. 269: 29382-29384.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29382-29384
    • Bjornstedt, M.1    Xue, J.2    Huang, W.3
  • 37
    • 0032080283 scopus 로고    scopus 로고
    • Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1
    • SAITOH, M., H. NISHITOH, M. FUJII, et al. 1998. Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBO J. 17: 2596-2606.
    • (1998) EMBO J. , vol.17 , pp. 2596-2606
    • Saitoh, M.1    Nishitoh, H.2    Fujii, M.3
  • 38
    • 0033569457 scopus 로고    scopus 로고
    • Phage display identifies thioredoxin and superoxide dismutase as novel protein kinase C-interacting proteins: Thioredoxin inhibits protein kinase C-mediated phosphorylation of histone
    • WATSON, J.A., M.G. RUMSBY & R.G. WOLOWACZ. 1999. Phage display identifies thioredoxin and superoxide dismutase as novel protein kinase C-interacting proteins: thioredoxin inhibits protein kinase C-mediated phosphorylation of histone. Biochem. J. 343: 301-305.
    • (1999) Biochem. J. , vol.343 , pp. 301-305
    • Watson, J.A.1    Rumsby, M.G.2    Wolowacz, R.G.3
  • 39
    • 0033521019 scopus 로고    scopus 로고
    • Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B
    • BARRETT, W.C., J.P. DEGNORE, Y.F. KENG, et al. 1999. Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B. J. Biol. Chem. 274: 34543-34546.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34543-34546
    • Barrett, W.C.1    DeGnore, J.P.2    Keng, Y.F.3
  • 40
    • 0029106436 scopus 로고
    • Thioredoxin h is one of the major proteins in rice phloem sap.
    • ISHIWATARI, Y., C. HONDA, I. KAWASHIMA, et al. 1995. Thioredoxin h is one of the major proteins in rice phloem sap. Planta 195: 456-463.
    • (1995) Planta , vol.195 , pp. 456-463
    • Ishiwatari, Y.1    Honda, C.2    Kawashima, I.3


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