메뉴 건너뛰기




Volumn 14, Issue 4, 2013, Pages 8073-8092

A differential redox regulation of the pathways metabolizing glyceraldehyde-3-phosphate tunes the production of reducing power in the cytosol of plant cells

Author keywords

Atp production; Nadph generation; Plant glycolysis; Redox regulation; Triose phosphate dehydrogenase

Indexed keywords

GLYCERALDEHYDE 3 PHOSPHATE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; THIOREDOXIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE (NADP); RECOMBINANT PROTEIN; VEGETABLE PROTEIN;

EID: 84877067606     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms14048073     Document Type: Article
Times cited : (37)

References (43)
  • 1
    • 0032773599 scopus 로고    scopus 로고
    • Evolving concepts in plant glycolysis: Two centuries of progress
    • Givan, C.V. Evolving concepts in plant glycolysis: Two centuries of progress. Biol. Rev. 1999, 74, 277-309.
    • (1999) Biol. Rev , vol.74 , pp. 277-309
    • Givan, C.V.1
  • 2
    • 0001259453 scopus 로고    scopus 로고
    • The Organization and regulation of plant glycolysis
    • Plaxton, W.C. The Organization and regulation of plant glycolysis. Annu. Rev. Plant Physiol. Plant Mol. Biol. 1996, 47, 185-214.
    • (1996) Annu. Rev. Plant Physiol. Plant Mol. Biol , vol.47 , pp. 185-214
    • Plaxton, W.C.1
  • 3
    • 0005138153 scopus 로고
    • On the metabolism of triose-phosphates in photosynthetic cells. Their involvement on the trafic of ATP and NADPH
    • Iglesias, A.A. On the metabolism of triose-phosphates in photosynthetic cells. Their involvement on the trafic of ATP and NADPH. Biochem. Educ. 1990, 18, 1-4.
    • (1990) Biochem. Educ , vol.18 , pp. 1-4
    • Iglesias, A.A.1
  • 4
    • 39149091761 scopus 로고    scopus 로고
    • Involvement of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase in response to oxidative stress
    • Bustos, D.M.; Bustamante, C.A.; Iglesias, A.A. Involvement of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase in response to oxidative stress. J. Plant Physiol. 2008, 165, 456-461.
    • (2008) J. Plant Physiol , vol.165 , pp. 456-461
    • Bustos, D.M.1    Bustamante, C.A.2    Iglesias, A.A.3
  • 5
    • 0037163878 scopus 로고    scopus 로고
    • Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase is post-translationally phosphorylated in heterotrophic cells of wheat (Triticum aestivum)
    • Bustos, D.M.; Iglesias, A.A. Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase is post-translationally phosphorylated in heterotrophic cells of wheat (Triticum aestivum). FEBS Lett. 2002, 530, 169-173.
    • (2002) FEBS Lett , vol.530 , pp. 169-173
    • Bustos, D.M.1    Iglesias, A.A.2
  • 6
    • 0347051814 scopus 로고    scopus 로고
    • Phosphorylated non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from heterotrophic cells of wheat interacts with 14-3-3 proteins
    • Bustos, D.M.; Iglesias, A.A. Phosphorylated non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from heterotrophic cells of wheat interacts with 14-3-3 proteins. Plant Physiol. 2003, 133, 2081-2088.
    • (2003) Plant Physiol , vol.133 , pp. 2081-2088
    • Bustos, D.M.1    Iglesias, A.A.2
  • 7
    • 79960145005 scopus 로고    scopus 로고
    • Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase is phosphorylated in wheat endosperm at Ser404 by a SNF1-related protein kinase allosterically inhibited by ribose 5 phosphate
    • Piattoni, C.V.; Bustos, D.M.; Guerrero, S.A.; Iglesias, A.A. Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase is phosphorylated in wheat endosperm at Ser404 by a SNF1-related protein kinase allosterically inhibited by ribose 5 phosphate. Plant Physiol. 2011, 156, 1337-1350.
    • (2011) Plant Physiol , vol.156 , pp. 1337-1350
    • Piattoni, C.V.1    Bustos, D.M.2    Guerrero, S.A.3    Iglesias, A.A.4
  • 8
    • 33747624376 scopus 로고    scopus 로고
    • Characterization of an Arabidopsis thaliana mutant lacking a cytosolic non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
    • Rius, S.P.; Casati, P.; Iglesias, A.A.; Gomez-Casati, D.F. Characterization of an Arabidopsis thaliana mutant lacking a cytosolic non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase. Plant Mol. Biol. 2006, 61, 945-957.
    • (2006) Plant Mol. Biol , vol.61 , pp. 945-957
    • Rius, S.P.1    Casati, P.2    Iglesias, A.A.3    Gomez-Casati, D.F.4
  • 9
    • 34548190012 scopus 로고    scopus 로고
    • A central integrator of transcription networks in plant stress and energy signalling
    • Baena-Gonzalez, E.; Rolland, F.; Thevelein, J.M.; Sheen, J. A central integrator of transcription networks in plant stress and energy signalling. Nature 2007, 448, 938-942.
    • (2007) Nature , vol.448 , pp. 938-942
    • Baena-Gonzalez, E.1    Rolland, F.2    Thevelein, J.M.3    Sheen, J.4
  • 10
    • 84864327019 scopus 로고    scopus 로고
    • Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the model plant Arabidopsis thaliana is reversed by both glutaredoxins and thioredoxins in vitro
    • Bedhomme, M.; Adamo, M.; Marchand, C.H.; Couturier, J.; Rouhier, N.; Lemaire, S.D.; Zaffagnini, M.; Trost, P. Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the model plant Arabidopsis thaliana is reversed by both glutaredoxins and thioredoxins in vitro. Biochem. J. 2012, 445, 337-347.
    • (2012) Biochem. J , vol.445 , pp. 337-347
    • Bedhomme, M.1    Adamo, M.2    Marchand, C.H.3    Couturier, J.4    Rouhier, N.5    Lemaire, S.D.6    Zaffagnini, M.7    Trost, P.8
  • 11
    • 28444491773 scopus 로고    scopus 로고
    • Proteomic identification of glyceraldehyde 3-phosphate dehydrogenase as an inhibitory target of hydrogen peroxide in Arabidopsis
    • Hancock, J.T.; Henson, D.; Nyirenda, M.; Desikan, R.; Harrison, J.; Lewis, M.; Hughes, J.; Neill, S.J. Proteomic identification of glyceraldehyde 3-phosphate dehydrogenase as an inhibitory target of hydrogen peroxide in Arabidopsis. Plant Physiol. Biochem. 2005, 43, 828-835.
    • (2005) Plant Physiol. Biochem , vol.43 , pp. 828-835
    • Hancock, J.T.1    Henson, D.2    Nyirenda, M.3    Desikan, R.4    Harrison, J.5    Lewis, M.6    Hughes, J.7    Neill, S.J.8
  • 13
    • 57749121325 scopus 로고    scopus 로고
    • Characterization of Arabidopsis lines deficient in GAPC-1, a cytosolic NAD-dependent glyceraldehyde-3-phosphate dehydrogenase
    • Rius, S.P.; Casati, P.; Iglesias, A.A.; Gomez-Casati, D.F. Characterization of Arabidopsis lines deficient in GAPC-1, a cytosolic NAD-dependent glyceraldehyde-3-phosphate dehydrogenase. Plant Physiol. 2008, 148, 1655-1667.
    • (2008) Plant Physiol , vol.148 , pp. 1655-1667
    • Rius, S.P.1    Casati, P.2    Iglesias, A.A.3    Gomez-Casati, D.F.4
  • 14
    • 77953534543 scopus 로고    scopus 로고
    • Heterologous expression of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Triticum aestivum and Arabidopsis thaliana
    • Piattoni, C.V.; Rius, S.P.; Gomez-Casati, D.F.; Guerrero, S.A.; Iglesias, A.A. Heterologous expression of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Triticum aestivum and Arabidopsis thaliana. Biochimie 2010, 92, 909-913.
    • (2010) Biochimie , vol.92 , pp. 909-913
    • Piattoni, C.V.1    Rius, S.P.2    Gomez-Casati, D.F.3    Guerrero, S.A.4    Iglesias, A.A.5
  • 15
    • 0014349341 scopus 로고
    • D-glyceraldehyde 3-phosphate dehydrogenases of higher plants
    • Schulman, M.D.; Gibbs, M. D-glyceraldehyde 3-phosphate dehydrogenases of higher plants. Plant Physiol. 1968, 43, 1805-1812.
    • (1968) Plant Physiol , vol.43 , pp. 1805-1812
    • Schulman, M.D.1    Gibbs, M.2
  • 16
    • 73649151319 scopus 로고
    • Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase
    • Kitz, R.; Wilson, I.B. Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase. J. Biol. Chem. 1962, 237, 3245-3249.
    • (1962) J. Biol. Chem , vol.237 , pp. 3245-3249
    • Kitz, R.1    Wilson, I.B.2
  • 17
    • 0035471025 scopus 로고    scopus 로고
    • Study of the properties of phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase
    • Nagradova, N.K. Study of the properties of phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 2001, 66, 1067-1076.
    • (2001) Biochemistry , vol.66 , pp. 1067-1076
    • Nagradova, N.K.1
  • 18
    • 0037131233 scopus 로고    scopus 로고
    • Characterization of the amino acids involved in substrate specificity of nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans
    • Marchal, S.; Branlant, G. Characterization of the amino acids involved in substrate specificity of nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans. J. Biol. Chem. 2002, 277, 39235-39242.
    • (2002) J. Biol. Chem , vol.277 , pp. 39235-39242
    • Marchal, S.1    Branlant, G.2
  • 20
    • 38149141701 scopus 로고    scopus 로고
    • Hydrogen peroxide in plants: A versatile molecule of the reactive oxygen species network
    • Quan, L.J.; Zhang, B.; Shi, W.W.; Li, H.Y. Hydrogen peroxide in plants: A versatile molecule of the reactive oxygen species network. J. Integr. Plant Biol. 2008, 50, 2-18.
    • (2008) J. Integr. Plant Biol , vol.50 , pp. 2-18
    • Quan, L.J.1    Zhang, B.2    Shi, W.W.3    Li, H.Y.4
  • 21
    • 85014109854 scopus 로고    scopus 로고
    • Biochemical Mechanisms for the Maintenance of Oxidative Stress under Control in Plants
    • Third Edition; Pessarakli, M., Ed.; Taylor and Francis Group, LLC: Boca Raton, FL USA, Arias
    • Arias, D.G.; Piattoni, C.V.; Guerrero, S.A.; Iglesias, A.A. Biochemical Mechanisms for the Maintenance of Oxidative Stress under Control in Plants. In Handbook of Plant and Crop Stress, Third Edition; Pessarakli, M., Ed.; Taylor and Francis Group, LLC: Boca Raton, FL, USA, 2011; pp. 157-190.
    • (2011) Handbook of Plant and Crop Stress , pp. 157-190
    • Arias, D.G.1    Piattoni, C.V.2    Guerrero, S.A.3    Iglesias, A.A.4
  • 22
    • 20444426141 scopus 로고    scopus 로고
    • A model for the interaction between plant GAPN and 14-3-3zeta using protein-protein docking calculations, electrostatic potentials and kinetics
    • Bustos, D.M.; Iglesias, A.A. A model for the interaction between plant GAPN and 14-3-3zeta using protein-protein docking calculations, electrostatic potentials and kinetics. J. Mol. Graph. Model 2005, 23, 490-502.
    • (2005) J. Mol. Graph. Model , vol.23 , pp. 490-502
    • Bustos, D.M.1    Iglesias, A.A.2
  • 23
    • 34548845570 scopus 로고    scopus 로고
    • The active site cysteine of the proapoptotic protein glyceraldehyde-3-phosphate dehydrogenase is essential in oxidative stress-induced aggregation and cell death
    • Nakajima, H.; Amano, W.; Fujita, A.; Fukuhara, A.; Azuma, Y.T.; Hata, F.; Inui, T.; Takeuchi, T. The active site cysteine of the proapoptotic protein glyceraldehyde-3-phosphate dehydrogenase is essential in oxidative stress-induced aggregation and cell death. J. Biol. Chem. 2007, 282, 26562-26574.
    • (2007) J. Biol. Chem , vol.282 , pp. 26562-26574
    • Nakajima, H.1    Amano, W.2    Fujita, A.3    Fukuhara, A.4    Azuma, Y.T.5    Hata, F.6    Inui, T.7    Takeuchi, T.8
  • 27
    • 33746445177 scopus 로고    scopus 로고
    • Nitric oxide-GAPDH-Siah: A novel cell death cascade
    • Hara, M.R.; Snyder, S.H. Nitric oxide-GAPDH-Siah: A novel cell death cascade. Cell Mol. Neurobiol. 2006, 26, 527-538.
    • (2006) Cell Mol. Neurobiol , vol.26 , pp. 527-538
    • Hara, M.R.1    Snyder, S.H.2
  • 30
    • 79959226194 scopus 로고    scopus 로고
    • On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: Biochemical mechanisms and regulatory control
    • Sirover, M.A. On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: Biochemical mechanisms and regulatory control. Biochim. Biophys. Acta 2011, 1810, 741-751.
    • (2011) Biochim. Biophys. Acta , vol.1810 , pp. 741-751
    • Sirover, M.A.1
  • 31
    • 57649171241 scopus 로고    scopus 로고
    • Human glyceraldehyde-3-phosphate dehydrogenase plays a direct role in reactivating oxidized forms of the DNA repair enzyme APE1
    • Azam, S.; Jouvet, N.; Jilani, A.; Vongsamphanh, R.; Yang, X.; Yang, S.; Ramotar, D. Human glyceraldehyde-3-phosphate dehydrogenase plays a direct role in reactivating oxidized forms of the DNA repair enzyme APE1. J. Biol. Chem. 2008, 283, 30632-30641.
    • (2008) J. Biol. Chem , vol.283 , pp. 30632-30641
    • Azam, S.1    Jouvet, N.2    Jilani, A.3    Vongsamphanh, R.4    Yang, X.5    Yang, S.6    Ramotar, D.7
  • 35
    • 33750819157 scopus 로고    scopus 로고
    • Reactive oxygen species as signals that modulate plant stress responses and programmed cell death
    • Gechev, T.S.; van Breusegem, F.; Stone, J.M.; Denev, I.; Laloi, C. Reactive oxygen species as signals that modulate plant stress responses and programmed cell death. Bioessays 2006, 28, 1091-1101.
    • (2006) Bioessays , vol.28 , pp. 1091-1101
    • Gechev, T.S.1    van Breusegem, F.2    Stone, J.M.3    Denev, I.4    Laloi, C.5
  • 36
    • 33745587282 scopus 로고    scopus 로고
    • Doing the unexpected: Proteins involved in hydrogen peroxide perception
    • Hancock, J.; Desikan, R.; Harrison, J.; Bright, J.; Hooley, R.; Neill, S. Doing the unexpected: Proteins involved in hydrogen peroxide perception. J. Exp. Bot. 2006, 57, 1711-1718.
    • (2006) J. Exp. Bot , vol.57 , pp. 1711-1718
    • Hancock, J.1    Desikan, R.2    Harrison, J.3    Bright, J.4    Hooley, R.5    Neill, S.6
  • 37
    • 84863112816 scopus 로고    scopus 로고
    • Cytosolic glyceraldehyde-3-phosphate dehydrogenases interact with phospholipase ddelta to transduce hydrogen peroxide signals in the Arabidopsis response to stress
    • Guo, L.; Devaiah, S.P.; Narasimhan, R.; Pan, X.; Zhang, Y.; Zhang, W.; Wang, X. Cytosolic glyceraldehyde-3-phosphate dehydrogenases interact with phospholipase ddelta to transduce hydrogen peroxide signals in the Arabidopsis response to stress. Plant Cell 2012, 24, 2200-2212.
    • (2012) Plant Cell , vol.24 , pp. 2200-2212
    • Guo, L.1    Devaiah, S.P.2    Narasimhan, R.3    Pan, X.4    Zhang, Y.5    Zhang, W.6    Wang, X.7
  • 38
    • 84861678049 scopus 로고    scopus 로고
    • Redox-shuttling between chloroplast and cytosol: Integration of intra-chloroplast and extra-chloroplast metabolism
    • Taniguchi, M.; Miyake, H. Redox-shuttling between chloroplast and cytosol: Integration of intra-chloroplast and extra-chloroplast metabolism. Curr. Opin. Plant Biol. 2012, 15, 252-260.
    • (2012) Curr. Opin. Plant Biol , vol.15 , pp. 252-260
    • Taniguchi, M.1    Miyake, H.2
  • 39
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 40
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 41
    • 0343963061 scopus 로고    scopus 로고
    • Structural and kinetic characterization of NADP-dependent, non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from celery leaves
    • Gómez Casati, D.F.; Sesma, J.I.; Iglesias, A.A. Structural and kinetic characterization of NADP-dependent, non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from celery leaves. Plant Sci. 2000, 154, 107-115.
    • (2000) Plant Sci , vol.154 , pp. 107-115
    • Gómez casati, D.F.1    Sesma, J.I.2    Iglesias, A.A.3
  • 42
    • 4243241375 scopus 로고
    • Determination of co-factor dissociation constants from the kinetics of inhibition of enzymes
    • Mildvan, A.S.; Leigh, R.A. Determination of co-factor dissociation constants from the kinetics of inhibition of enzymes. Biochim. Biophys. Acta 1964, 89, 393-397.
    • (1964) Biochim. Biophys. Acta , vol.89 , pp. 393-397
    • Mildvan, A.S.1    Leigh, R.A.2
  • 43
    • 49749177569 scopus 로고
    • A colorimetric method for determining low concentrations of mercaptans
    • Ellman, G.L. A colorimetric method for determining low concentrations of mercaptans. Arch. Biochem. Biophys. 1958, 74, 443-450.
    • (1958) Arch. Biochem. Biophys , vol.74 , pp. 443-450
    • Ellman, G.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.