메뉴 건너뛰기




Volumn 150, Issue 2, 2009, Pages 552-561

Heat-shock and redox-dependent functional switching of an h-type arabidopsis thioredoxin from a disulfide reductase to a molecular chaperone

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA;

EID: 66649083429     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.109.135426     Document Type: Article
Times cited : (109)

References (46)
  • 1
    • 0028384702 scopus 로고
    • Transient transformation of Arabidopsis leaf protoplasts: A versatile experimental system to study gene expression
    • Abel S, Theologis A (1994) Transient transformation of Arabidopsis leaf protoplasts: a versatile experimental system to study gene expression. Plant J 5: 421-427
    • (1994) Plant J , vol.5 , pp. 421-427
    • Abel, S.1    Theologis, A.2
  • 2
    • 0030671351 scopus 로고    scopus 로고
    • Human thioredoxin homodimers: Regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60 -> asparagine mutant
    • Andersen JF, Sanders DA, Gasdaska JR, Weichsel A, Powis G, Montfort WR (1997) Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60 -> asparagine mutant. Biochemistry 36:13979-13988
    • (1997) Biochemistry , vol.36 , pp. 13979-13988
    • Andersen, J.F.1    Sanders, D.A.2    Gasdaska, J.R.3    Weichsel, A.4    Powis, G.5    Montfort, W.R.6
  • 3
    • 0033582933 scopus 로고    scopus 로고
    • Bridge over troubled waters: Sensing stress by disulfide bond formation
    • Aslund F, Beckwith J (1999) Bridge over troubled waters: sensing stress by disulfide bond formation. Cell 96: 751-753
    • (1999) Cell , vol.96 , pp. 751-753
    • Aslund, F.1    Beckwith, J.2
  • 6
    • 33644559039 scopus 로고    scopus 로고
    • The antioxidant protein alkylhydroperoxide reductase of Helicobacter pylori switches from a peroxide reductase to a molecular chaperone function
    • Chuang MH, Wu MS, Lo WL, Lin JT, Wong CH, Chiou SH (2006) The antioxidant protein alkylhydroperoxide reductase of Helicobacter pylori switches from a peroxide reductase to a molecular chaperone function. Proc Natl Acad Sci USA 103: 2552-2557
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2552-2557
    • Chuang, M.H.1    Wu, M.S.2    Lo, W.L.3    Lin, J.T.4    Wong, C.H.5    Chiou, S.H.6
  • 7
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough SJ, Bent AF (1998) Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J 16: 735-743
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 8
    • 0033521012 scopus 로고    scopus 로고
    • Differential temperature-dependent chaperonelike activity of alphaA- and alphaB-crystallin homoaggregates
    • Datta SA, Rao CM (1999) Differential temperature-dependent chaperonelike activity of alphaA- and alphaB-crystallin homoaggregates. J Biol Chem 274: 34773-34778
    • (1999) J Biol Chem , vol.274 , pp. 34773-34778
    • Datta, S.A.1    Rao, C.M.2
  • 9
    • 0029899159 scopus 로고    scopus 로고
    • Oxidative stress is involved in heat-induced cell death in Saccharomyces cerevisiae
    • Davidson JF, Whyte B, Bissinger PH, Schiestl RH (1996) Oxidative stress is involved in heat-induced cell death in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 93: 5116-5121
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5116-5121
    • Davidson, J.F.1    Whyte, B.2    Bissinger, P.H.3    Schiestl, R.H.4
  • 10
    • 0031024788 scopus 로고    scopus 로고
    • Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: Structural and functional characterization of mutants of Asp 26 and Lys 57
    • Dyson HJ, Jeng MF, Tennant LL, Slaby I, Lindell M, Cui DS, Kuprin S, Holmgren A (1997) Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: structural and functional characterization of mutants of Asp 26 and Lys 57. Biochemistry 36: 2622-2636
    • (1997) Biochemistry , vol.36 , pp. 2622-2636
    • Dyson, H.J.1    Jeng, M.F.2    Tennant, L.L.3    Slaby, I.4    Lindell, M.5    Cui, D.S.6    Kuprin, S.7    Holmgren, A.8
  • 11
    • 0030933301 scopus 로고    scopus 로고
    • A permeabilized cell system, that assembles filamentous bacteriophage
    • Feng JN, Russel M, Model P (1997) A permeabilized cell system, that assembles filamentous bacteriophage. Proc Natl Acad Sci USA 94: 4068-4073
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4068-4073
    • Feng, J.N.1    Russel, M.2    Model, P.3
  • 14
    • 0032549677 scopus 로고    scopus 로고
    • The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure
    • Haley DA, Horwitz J, Stewart PL (1998) The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure. J Mol Biol 277: 27-35
    • (1998) J Mol Biol , vol.277 , pp. 27-35
    • Haley, D.A.1    Horwitz, J.2    Stewart, P.L.3
  • 15
    • 17044382971 scopus 로고    scopus 로고
    • A unique loop in T7 DNA polymerase mediates the binding of helicase-primase, DNA binding protein, and processivity factor
    • Hamdan SM, Marintcheva B, Cook T, Lee SJ, Tabor S, Richardson CC (2005) A unique loop in T7 DNA polymerase mediates the binding of helicase-primase, DNA binding protein, and processivity factor. Proc Natl Acad Sci USA 102: 5096-5101
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5096-5101
    • Hamdan, S.M.1    Marintcheva, B.2    Cook, T.3    Lee, S.J.4    Tabor, S.5    Richardson, C.C.6
  • 18
    • 0029187491 scopus 로고
    • Thioredoxin and thioredoxin reductase
    • Holmgren A, Bjornstedt M (1995) Thioredoxin and thioredoxin reductase. Methods Enzymol 252:199-208
    • (1995) Methods Enzymol , vol.252 , pp. 199-208
    • Holmgren, A.1    Bjornstedt, M.2
  • 20
    • 2542464938 scopus 로고    scopus 로고
    • Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function
    • Jang HH, Lee KO, Chi YH, Jung BG, Park SK, Park JH, Lee JR, Lee SS, Moon JC, Yun JW, et al (2004) Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function. Cell 117: 625-635
    • (2004) Cell , vol.117 , pp. 625-635
    • Jang, H.H.1    Lee, K.O.2    Chi, Y.H.3    Jung, B.G.4    Park, S.K.5    Park, J.H.6    Lee, J.R.7    Lee, S.S.8    Moon, J.C.9    Yun, J.W.10
  • 21
    • 0025319619 scopus 로고
    • Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution
    • Katti SK, LeMaster DM, Eklund H (1990) Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution. J Mol Biol 212: 167-184
    • (1990) J Mol Biol , vol.212 , pp. 167-184
    • Katti, S.K.1    LeMaster, D.M.2    Eklund, H.3
  • 22
    • 0038245262 scopus 로고    scopus 로고
    • Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase
    • Kern R, Malki A, Holmgren A, Richarme G (2003) Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase. Biochem J 371: 965-972
    • (2003) Biochem J , vol.371 , pp. 965-972
    • Kern, R.1    Malki, A.2    Holmgren, A.3    Richarme, G.4
  • 23
    • 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
  • 25
    • 0027203922 scopus 로고
    • The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity
    • LaMantia ML, Lennarz WJ (1993) The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity. Cell 74: 899-908
    • (1993) Cell , vol.74 , pp. 899-908
    • LaMantia, M.L.1    Lennarz, W.J.2
  • 28
    • 33750013432 scopus 로고    scopus 로고
    • Formation, TEM study and 3D reconstruction of the human erythrocyte peroxiredoxin-2 dodecahedral higher-order assembly
    • Meissner U, Schröder E, Scheffler D, Martin AG, Harris JR (2007) Formation, TEM study and 3D reconstruction of the human erythrocyte peroxiredoxin-2 dodecahedral higher-order assembly. Micron 38:29-39
    • (2007) Micron , vol.38 , pp. 29-39
    • Meissner, U.1    Schröder, E.2    Scheffler, D.3    Martin, A.G.4    Harris, J.R.5
  • 29
    • 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
  • 32
    • 26044440113 scopus 로고
    • Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophyll a and b extracted with four different solvents: Verification of the concentration of chlorophyll standards by atomic absorption spectroscopy
    • Porra RJ, Thompson WA, Kriedemann PE (1989) Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophyll a and b extracted with four different solvents: verification of the concentration of chlorophyll standards by atomic absorption spectroscopy. Biochim Biophys Acta 975: 384-394
    • (1989) Biochim Biophys Acta , vol.975 , pp. 384-394
    • Porra, R.J.1    Thompson, W.A.2    Kriedemann, P.E.3
  • 33
    • 0029146852 scopus 로고
    • Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site
    • Quan H, Fan G, Wang CC (1995) Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site. J Biol Chem 270:17078-17080
    • (1995) J Biol Chem , vol.270 , pp. 17078-17080
    • Quan, H.1    Fan, G.2    Wang, C.C.3
  • 34
    • 28844443129 scopus 로고    scopus 로고
    • Endogenous thioredoxin is required for redox cycling of anthracyclines and p53-dependent apoptosis in cancer cells
    • Ravi D, Muniyappa H, Das KC (2005) Endogenous thioredoxin is required for redox cycling of anthracyclines and p53-dependent apoptosis in cancer cells. J Biol Chem 280: 40084-40096
    • (2005) J Biol Chem , vol.280 , pp. 40084-40096
    • Ravi, D.1    Muniyappa, H.2    Das, K.C.3
  • 35
    • 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
  • 36
    • 0042209787 scopus 로고    scopus 로고
    • Type-h thioredoxins accumulate in the nucleus of developing wheat seed tissues suffering oxidative stress
    • Serrato AJ, Cejudo FJ (2003) Type-h thioredoxins accumulate in the nucleus of developing wheat seed tissues suffering oxidative stress. Planta 217: 392-399
    • (2003) Planta , vol.217 , pp. 392-399
    • Serrato, A.J.1    Cejudo, F.J.2
  • 38
    • 0032502739 scopus 로고    scopus 로고
    • Interaction of l,l'-bi(4anilino)naphthalene-5,5'-disulfonic acid, with alpha-crystallin
    • Sharma KK, Kaur H, Kumar GS, Kester K (1998) Interaction of l,l'-bi(4anilino)naphthalene-5,5'-disulfonic acid, with alpha-crystallin. J Biol Chem 273: 8965-8970
    • (1998) J Biol Chem , vol.273 , pp. 8965-8970
    • Sharma, K.K.1    Kaur, H.2    Kumar, G.S.3    Kester, K.4
  • 39
    • 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
  • 40
  • 41
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • The Arabidopsis Genome Initiative
    • The Arabidopsis Genome Initiative (2000) Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 408: 796-815
    • (2000) Nature , vol.408 , pp. 796-815
  • 42
    • 0030585429 scopus 로고    scopus 로고
    • Crystal structures of reduced, oxidized, and mutated human thioredoxins: Evidence for a regulatory homodimer
    • Weichsel A, Gasdaska JR, Powis G, Montfort WR (1996) Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. Structure 4: 735-751
    • (1996) Structure , vol.4 , pp. 735-751
    • Weichsel, A.1    Gasdaska, J.R.2    Powis, G.3    Montfort, W.R.4
  • 43
    • 0023685552 scopus 로고    scopus 로고
    • Wollman EE, d'Auriol L, Rimsky L, Shaw A, Jacquot JP, Wingfield P, Graber P, Dessarps F, Robin P, Galibert F, et al (1988) Cloning and expression of a cDNA for human thioredoxin. J Biol Chem 263:1550615512
    • Wollman EE, d'Auriol L, Rimsky L, Shaw A, Jacquot JP, Wingfield P, Graber P, Dessarps F, Robin P, Galibert F, et al (1988) Cloning and expression of a cDNA for human thioredoxin. J Biol Chem 263:1550615512
  • 45
    • 0037418896 scopus 로고    scopus 로고
    • A stress sensor for the bacterial periplasm
    • Young JC, Hartl FU (2003) A stress sensor for the bacterial periplasm. Cell 113: 1-2
    • (2003) Cell , vol.113 , pp. 1-2
    • Young, J.C.1    Hartl, F.U.2
  • 46
    • 17144364275 scopus 로고    scopus 로고
    • Zhao TJ, Ou WB, Xie Q, Liu Y, Yan YB, Zhou HM (2005) Catalysis of creatine kinase refolding by protein disulfide isomerase involves disulfide cross-link and dimer to tetramer switch. J Biol Chem 280: 1347013476
    • Zhao TJ, Ou WB, Xie Q, Liu Y, Yan YB, Zhou HM (2005) Catalysis of creatine kinase refolding by protein disulfide isomerase involves disulfide cross-link and dimer to tetramer switch. J Biol Chem 280: 1347013476


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.