메뉴 건너뛰기




Volumn 106, Issue 14, 2009, Pages 5978-5983

Heat-shock dependent oligomeric status alters the function of a plant-specific thioredoxin-like protein, AtTDX

Author keywords

Disulfide reductase; Foldase chaperone; Holdase chaperone functional switching; Yedox

Indexed keywords

THIOREDOXIN;

EID: 65249186736     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0811231106     Document Type: Article
Times cited : (97)

References (36)
  • 1
    • 0031024788 scopus 로고    scopus 로고
    • Effectsofburied charged groups oncysteine thiol ionization and reactivity in Escherichia coli thioredoxin: Structural and functional characterization of mutants of Asp-26 and Lys-57
    • Dyson HJ, etal. (1997) Effectsofburied charged groups oncysteine 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
  • 2
    • 0030933301 scopus 로고    scopus 로고
    • A permeabilized cell system that assembles filamentous bacteriophage
    • Feng JN, et al. (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
  • 3
    • 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, et al. (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
  • 4
    • 0031028975 scopus 로고    scopus 로고
    • Cloning and expressionofanovel mammalian thioredoxin
    • SpyrouG, etal. (1997) Cloning and expressionofanovel mammalian thioredoxin. J Biol Chem 272:2936-2941.
    • (1997) J Biol Chem , vol.272 , pp. 2936-2941
    • Spyrou, G.1
  • 5
    • 0023685552 scopus 로고
    • Cloning and expression of a cDNA for human thioredoxin
    • Wollman EE, et al. (1988) Cloning and expression of a cDNA for human thioredoxin. J Biol Chem 263:15506-15512.
    • (1988) J Biol Chem , vol.263 , pp. 15506-15512
    • Wollman, E.E.1
  • 6
    • 0026020092 scopus 로고
    • Yeast thioredoxin genes
    • Gan ZR (1991) Yeast thioredoxin genes. J Biol Chem 266:1692-1696.
    • (1991) J Biol Chem , vol.266 , pp. 1692-1696
    • Gan, Z.R.1
  • 7
    • 0033525509 scopus 로고    scopus 로고
    • Identification and functional characterization of a novel mitochondrial thioredoxin system in Saccharomyces cerevisiae
    • Pedrajas JR, et al. (1999) Identification and functional characterization of a novel mitochondrial thioredoxin system in Saccharomyces cerevisiae. J Biol Chem 274:6366-6373.
    • (1999) J Biol Chem , vol.274 , pp. 6366-6373
    • Pedrajas, J.R.1
  • 8
    • 33645951646 scopus 로고    scopus 로고
    • The Escherichia coli thioredoxin homolog YbbN/Trxsc is a chaperone and a weak protein oxidoreductase
    • Caldas T, et al. (2006) The Escherichia coli thioredoxin homolog YbbN/Trxsc is a chaperone and a weak protein oxidoreductase. Biochem Biophys Res Commun 343:780-786.
    • (2006) Biochem Biophys Res Commun , vol.343 , pp. 780-786
    • Caldas, T.1
  • 9
    • 0036119804 scopus 로고    scopus 로고
    • Classification of plant thioredoxins by sequence similarity and intron position
    • Meyer Y, et al. (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
  • 10
    • 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
  • 11
    • 0029830772 scopus 로고    scopus 로고
    • Three members of a novel small gene-family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity encode proteins with a thioredoxin-like domain and ''APS reductase'' activity
    • Gutierrez-Marcos JF, et al. (1996) Three members of a novel small gene-family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity encode proteins with a thioredoxin-like domain and ''APS reductase'' activity. Proc Natl Acad Sci USA 93:13377-13382.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13377-13382
    • Gutierrez-Marcos, J.F.1
  • 12
    • 19044379862 scopus 로고    scopus 로고
    • Phylogenetic analyses identify 10 classes of the protein disulfide isomerase family in plants, including single-domain protein disulfide isomerase-related proteins
    • Houston NL, et al. (2005) Phylogenetic analyses identify 10 classes of the protein disulfide isomerase family in plants, including single-domain protein disulfide isomerase-related proteins. Plant Physiol 137:762-778.
    • (2005) Plant Physiol , vol.137 , pp. 762-778
    • Houston, N.L.1
  • 13
    • 0034695550 scopus 로고    scopus 로고
    • Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain
    • Witte S, et al. (2000) Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain. J Biol Chem 275:1902-1909.
    • (2000) J Biol Chem , vol.275 , pp. 1902-1909
    • Witte, S.1
  • 14
    • 2542464938 scopus 로고    scopus 로고
    • Two enzymes in one, two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to amolecular chaperone function
    • Jang HH, et al. (2004) Two enzymes in one, two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to amolecular chaperone function. Cell 117:625-635.
    • (2004) Cell , vol.117 , pp. 625-635
    • Jang, H.H.1
  • 15
    • 33750013432 scopus 로고    scopus 로고
    • Formation, TEM study, and 3D reconstruction of the human erythrocyte peroxiredoxin-2 dodecahedral higher-order assembly
    • Meissner U, et al. (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
  • 16
    • 0037799277 scopus 로고    scopus 로고
    • Redox control of Hsp70-Co-chaperone interaction revealed by expression of a thioredoxin-like Arabidopsis protein
    • Vignols F, et al. (2003) Redox control of Hsp70-Co-chaperone interaction revealed by expression of a thioredoxin-like Arabidopsis protein. J Biol Chem 278:4516-4523.
    • (2003) J Biol Chem , vol.278 , pp. 4516-4523
    • Vignols, F.1
  • 17
    • 0344496513 scopus 로고    scopus 로고
    • The tetratricopeptide repeat: A structural motif mediating protein-protein interactions
    • Blatch GL, Lassle M (1999) The tetratricopeptide repeat: A structural motif mediating protein-protein interactions. BioEssays 21:932-939.
    • (1999) BioEssays , vol.21 , pp. 932-939
    • Blatch, G.L.1    Lassle, M.2
  • 18
    • 0031946770 scopus 로고    scopus 로고
    • How chaperones fold proteins
    • Beissinger M, Buchner J (1998) How chaperones fold proteins. Biol Chem 379:245-259.
    • (1998) Biol Chem , vol.379 , pp. 245-259
    • Beissinger, M.1    Buchner, J.2
  • 19
    • 0038245262 scopus 로고    scopus 로고
    • Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase
    • Kern R, et al. (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
  • 20
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • Tsai B, et al. (2001) Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell 104:937-948.
    • (2001) Cell , vol.104 , pp. 937-948
    • Tsai, B.1
  • 21
    • 0027507970 scopus 로고
    • Thermal switching between enhanced and arrested reactivation of bacterial glucose-6-phosphate dehydrogenase assisted by GroEL in the absence of ATP
    • Hansen JE, Gafni A (1993) Thermal switching between enhanced and arrested reactivation of bacterial glucose-6-phosphate dehydrogenase assisted by GroEL in the absence of ATP. J Biol Chem 268:21632-21636.
    • (1993) J Biol Chem , vol.268 , pp. 21632-21636
    • Hansen, J.E.1    Gafni, A.2
  • 22
    • 4644313922 scopus 로고    scopus 로고
    • A domain in the N-terminal part of Hsp26 is essential for chaperone function and oligomerization
    • Haslbeck M, et al. (2004) A domain in the N-terminal part of Hsp26 is essential for chaperone function and oligomerization. J Mol Biol 343:445-455.
    • (2004) J Mol Biol , vol.343 , pp. 445-455
    • Haslbeck, M.1
  • 23
    • 0019728717 scopus 로고
    • Use of multivariate statistics in analyzing the images of biological macromolecules
    • van Heel M, Frank J (1981) Use of multivariate statistics in analyzing the images of biological macromolecules. Ultramicroscopy 6:187-194.
    • (1981) Ultramicroscopy , vol.6 , pp. 187-194
    • van Heel, M.1    Frank, J.2
  • 24
    • 48949120180 scopus 로고    scopus 로고
    • Arabidopsis stromal 70-kD heat shock proteins are essential for plant development and important for thermotolerance of germinating seeds
    • Su PH, Li HM (2008) Arabidopsis stromal 70-kD heat shock proteins are essential for plant development and important for thermotolerance of germinating seeds. Plant Physiol 146:1231-1241.
    • (2008) Plant Physiol , vol.146 , pp. 1231-1241
    • Su, P.H.1    Li, H.M.2
  • 25
    • 0034119621 scopus 로고    scopus 로고
    • Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis
    • Queitsch C, etal. (2000) Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis. Plant Cell 12:479-492.
    • (2000) Plant Cell , vol.12 , pp. 479-492
    • Queitsch, C.1
  • 26
    • 0028321726 scopus 로고
    • Protein disulfide isomerase exhibits chaperone and antichaperone activity in the oxidative refolding of lysozyme
    • Puig A, Gilbert HF (1994) Protein disulfide isomerase exhibits chaperone and antichaperone activity in the oxidative refolding of lysozyme. J Biol Chem 269:7764-7771.
    • (1994) J Biol Chem , vol.269 , pp. 7764-7771
    • Puig, A.1    Gilbert, H.F.2
  • 27
    • 17144364275 scopus 로고    scopus 로고
    • Catalysis of creatine kinase refolding by protein disulfide isomerase involves disulfide cross-link and dimer to tetramer switch
    • Zhao TJ, et al. (2005) Catalysis of creatine kinase refolding by protein disulfide isomerase involves disulfide cross-link and dimer to tetramer switch. J Biol Chem 280:13470-13476.
    • (2005) J Biol Chem , vol.280 , pp. 13470-13476
    • Zhao, T.J.1
  • 28
    • 0026070055 scopus 로고
    • A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase
    • Meyer-Siegler K, et al. (1991) A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase. Proc Natl Acad Sci USA 88:8460-8464.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8460-8464
    • Meyer-Siegler, K.1
  • 29
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell DA, et al. (1994) Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372:475-478.
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1
  • 30
    • 34248183000 scopus 로고    scopus 로고
    • Proteomics uncovers a role for redox in drought tolerance in wheat
    • Hajheidari M, et al. (2007) Proteomics uncovers a role for redox in drought tolerance in wheat. J Proteome Res 6:1451-1460.
    • (2007) J Proteome Res , vol.6 , pp. 1451-1460
    • Hajheidari, M.1
  • 31
    • 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
  • 32
    • 4544356426 scopus 로고    scopus 로고
    • Oligomerization, chaperone activity, and nuclear localization of p26, a small heat shock protein from Artemia franciscana
    • Sun Y, et al. (2004) Oligomerization, chaperone activity, and nuclear localization of p26, a small heat shock protein from Artemia franciscana. J Biol Chem 279:39999-40006.
    • (2004) J Biol Chem , vol.279 , pp. 39999-40006
    • Sun, Y.1
  • 33
    • 0032502739 scopus 로고    scopus 로고
    • Interaction of 1,1'-bi(4-anilino) naphthalene-5,5'-disulfonic acid with α-crystallin
    • Sharma KK, et al. (1998) Interaction of 1,1'-bi(4-anilino) naphthalene-5,5'-disulfonic acid with α-crystallin. J Biol Chem 273:8965-8970.
    • (1998) J Biol Chem , vol.273 , pp. 8965-8970
    • Sharma, K.K.1
  • 34
    • 23344451043 scopus 로고    scopus 로고
    • Oxidative stress-dependent structural and functional switching of a human 2-Cys peroxiredoxin isotype II that enhances HeLa cell resistance to H2O2-induced cell death
    • Moon JC, et al. (2005) Oxidative stress-dependent structural and functional switching of a human 2-Cys peroxiredoxin isotype II that enhances HeLa cell resistance to H2O2-induced cell death. J Biol Chem 280:28775-28784.
    • (2005) J Biol Chem , vol.280 , pp. 28775-28784
    • Moon, J.C.1
  • 35
    • 33645728835 scopus 로고    scopus 로고
    • Oligomeric structure of the ATP-dependent protease La (Lon) of Escherichia coli
    • Park SC, et al. (2006) Oligomeric structure of the ATP-dependent protease La (Lon) of Escherichia coli. Mol Cells 21:129-134.
    • (2006) Mol Cells , vol.21 , pp. 129-134
    • Park, S.C.1
  • 36
    • 16544371166 scopus 로고    scopus 로고
    • Floral dip: Agrobacterium-mediatedgerm line transformation
    • CloughSJ
    • CloughSJ (2005) Floral dip: Agrobacterium-mediatedgerm line transformation. Methods Mol Biol 286:91-102.
    • (2005) Methods Mol Biol , vol.286 , pp. 91-102


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.