메뉴 건너뛰기




Volumn 1804, Issue 12, 2010, Pages 2213-2221

Redox properties of a thioredoxin-like Arabidopsis protein, AtTDX

Author keywords

Methoxyl PEG maleimide; Redox titrations; Tetratricopeptide repeating domain; Thioredoxin motif

Indexed keywords

BROMOBIMANE; CHAPERONE; CYSTINE; DISULFIDE; DITHIOL DERIVATIVE; MALEIMIDE DERIVATIVE; PROTEIN ATTDX; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; THIOREDOXIN; UNCLASSIFIED DRUG;

EID: 77957965148     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.09.005     Document Type: Article
Times cited : (11)

References (42)
  • 1
    • 42949151399 scopus 로고    scopus 로고
    • The ferredoxin/thioredoxin system of oxygenic photosynthesis
    • Schurmann P., Buchanan B.B. The ferredoxin/thioredoxin system of oxygenic photosynthesis. Antioxid. Redox Signal. 2008, 10:1235-1274.
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 1235-1274
    • Schurmann, P.1    Buchanan, B.B.2
  • 5
    • 0036119804 scopus 로고    scopus 로고
    • Classification of plant thioredoxins by sequence similarity and intron position
    • Meyer Y., Vignols F., Reichheld J.P. Classification of plant thioredoxins by sequence similarity and intron position. Methods Enzymol 2002, 347:394-402.
    • (2002) Methods Enzymol , vol.347 , pp. 394-402
    • Meyer, Y.1    Vignols, F.2    Reichheld, J.P.3
  • 7
    • 20044367629 scopus 로고    scopus 로고
    • Redox regulation: a broadening horizon
    • Buchanan B.B., Balmer Y. Redox regulation: a broadening horizon. Annu. Rev. Plant Biol. 2005, 56:187-220.
    • (2005) Annu. Rev. Plant Biol. , vol.56 , pp. 187-220
    • Buchanan, B.B.1    Balmer, Y.2
  • 8
    • 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 J.F., Roberts M.A., Campbell E.I., Wray J.L. 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. U. S. A. 1996, 93:13377-13382.
    • (1996) Proc. Natl Acad. Sci. U. S. A. , vol.93 , pp. 13377-13382
    • Gutierrez-Marcos, J.F.1    Roberts, M.A.2    Campbell, E.I.3    Wray, J.L.4
  • 9
    • 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 N.L., Fan C., Xiang J.Q., Schulze J.M., Jung R., Boston R.S. Phylogenetic analyses identify 10 classes of the protein disulfide isomerase family in plants, including single-domain protein disulfide isomerase-related proteins. Plant Physiol. 2005, 137:762-778.
    • (2005) Plant Physiol. , vol.137 , pp. 762-778
    • Houston, N.L.1    Fan, C.2    Xiang, J.Q.3    Schulze, J.M.4    Jung, R.5    Boston, R.S.6
  • 10
    • 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., Villalba M., Bi K., Liu Y., Isakov N., Altman A. 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. 2000, 275:1902-1909.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1902-1909
    • Witte, S.1    Villalba, M.2    Bi, K.3    Liu, Y.4    Isakov, N.5    Altman, A.6
  • 12
    • 33750013432 scopus 로고    scopus 로고
    • Formation, TEM study and 3D reconstruction of the human erythrocyte peroxiredoxin-2 dodecahedral higher-order assembly
    • Meissner U., Schroder E., Scheffler D., Martin A.G., Harris J.R. Formation, TEM study and 3D reconstruction of the human erythrocyte peroxiredoxin-2 dodecahedral higher-order assembly. Micron 2007, 38:29-39.
    • (2007) Micron , vol.38 , pp. 29-39
    • Meissner, U.1    Schroder, E.2    Scheffler, D.3    Martin, A.G.4    Harris, J.R.5
  • 13
    • 0037799277 scopus 로고    scopus 로고
    • Redox control of Hsp70-Co-chaperone interaction revealed by expression of a thioredoxin-like Arabidopsis protein
    • Vignols F., Mouaheb N., Thomas D., Meyer Y. Redox control of Hsp70-Co-chaperone interaction revealed by expression of a thioredoxin-like Arabidopsis protein. J. Biol. Chem. 2003, 278:4516-4523.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4516-4523
    • Vignols, F.1    Mouaheb, N.2    Thomas, D.3    Meyer, Y.4
  • 14
    • 34250838027 scopus 로고    scopus 로고
    • Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR
    • Volkov A.N., Worrall J.A., Holtzmann E., Ubbink M. Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR. Proc. Natl Acad. Sci. U. S. A. 2006, 103:18945-18950.
    • (2006) Proc. Natl Acad. Sci. U. S. A. , vol.103 , pp. 18945-18950
    • Volkov, A.N.1    Worrall, J.A.2    Holtzmann, E.3    Ubbink, M.4
  • 16
    • 0032473425 scopus 로고    scopus 로고
    • The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions
    • Das A.K., Cohen P.W., Barford D. The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBO J. 1998, 17:1192-1199.
    • (1998) EMBO J. , vol.17 , pp. 1192-1199
    • Das, A.K.1    Cohen, P.W.2    Barford, D.3
  • 17
    • 0344496513 scopus 로고    scopus 로고
    • The tetratricopeptide repeat: a structural motif mediating protein-protein interactions
    • Blatch G.L., Lassle M. The tetratricopeptide repeat: a structural motif mediating protein-protein interactions. Bioessays 1999, 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. How chaperones fold proteins. Biol. Chem. 1998, 379:245-259.
    • (1998) Biol. Chem. , vol.379 , pp. 245-259
    • Beissinger, M.1    Buchner, J.2
  • 19
    • 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
  • 20
    • 0032125811 scopus 로고    scopus 로고
    • The single mutation Trp35->Ala in the 35-40 redox site of Chlamydomonas reinhardtii thioredoxin h affects its biochemical activity and the pH dependence of C36-C39 1H-13C NMR
    • Krimm I., Lemaire S., Ruelland E., Miginiac-Maslow M., Jaquot J.P., Hirasawa M., Knaff D.B., Lancelin J.M. The single mutation Trp35->Ala in the 35-40 redox site of Chlamydomonas reinhardtii thioredoxin h affects its biochemical activity and the pH dependence of C36-C39 1H-13C NMR. Eur. J. Biochem. 1998, 255:185-195.
    • (1998) Eur. J. Biochem. , vol.255 , pp. 185-195
    • Krimm, I.1    Lemaire, S.2    Ruelland, E.3    Miginiac-Maslow, M.4    Jaquot, J.P.5    Hirasawa, M.6    Knaff, D.B.7    Lancelin, J.M.8
  • 21
    • 0040799938 scopus 로고    scopus 로고
    • Oxidation-reduction properties of chloroplast thioredoxins, ferredoxin:thioredoxin reductase, and thioredoxin f-regulated enzymes
    • Hirasawa M., Schurmann P., Jacquot J.P., Manieri W., Jacquot P., Keryer E., Hartman F.C., Knaff D.B. Oxidation-reduction properties of chloroplast thioredoxins, ferredoxin:thioredoxin reductase, and thioredoxin f-regulated enzymes. Biochemistry 1999, 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
  • 24
    • 15744380512 scopus 로고    scopus 로고
    • A structural disulfide of yeast protein-disulfide isomerase destabilizes the active site disulfide of the N-terminal thioredoxin domain
    • Wilkinson B., Xiao R., Gilbert H.F. A structural disulfide of yeast protein-disulfide isomerase destabilizes the active site disulfide of the N-terminal thioredoxin domain. J. Biol. Chem. 2005, 280:11483-11487.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11483-11487
    • Wilkinson, B.1    Xiao, R.2    Gilbert, H.F.3
  • 26
    • 6344282754 scopus 로고    scopus 로고
    • Properties of the cysteine residues and iron-sulfur cluster of the assimilatory 5'-adenylyl sulfate reductase from Pseudomonas aeruginosa
    • Kim S.K., Rahman A., Bick J.A., Conover R.C., Johnson M.K., Mason J.T., Hirasawa M., Leustek T., Knaff D.B. Properties of the cysteine residues and iron-sulfur cluster of the assimilatory 5'-adenylyl sulfate reductase from Pseudomonas aeruginosa. Biochemistry 2004, 43:13478-13486.
    • (2004) Biochemistry , vol.43 , pp. 13478-13486
    • Kim, S.K.1    Rahman, A.2    Bick, J.A.3    Conover, R.C.4    Johnson, M.K.5    Mason, J.T.6    Hirasawa, M.7    Leustek, T.8    Knaff, D.B.9
  • 27
    • 0025914427 scopus 로고
    • Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin
    • Krause G., Lundstrom J., Barea J.L., Pueyo de la Cuesta C., Holmgren A. Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin. J. Biol. Chem. 1991, 266:9494-9500.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9494-9500
    • Krause, G.1    Lundstrom, J.2    Barea, J.L.3    Pueyo de la Cuesta, C.4    Holmgren, A.5
  • 28
    • 0035909812 scopus 로고    scopus 로고
    • Oxidation-reduction and activation properties of chloroplast fructose 1, 6-bisphosphatase with mutated regulatory site
    • Balmer Y., Stritt-Etter A.L., Hirasawa M., Jacquot J.P., Keryer E., Knaff D.B., Schurmann P. Oxidation-reduction and activation properties of chloroplast fructose 1, 6-bisphosphatase with mutated regulatory site. Biochemistry 2001, 40:15444-15450.
    • (2001) Biochemistry , vol.40 , pp. 15444-15450
    • Balmer, Y.1    Stritt-Etter, A.L.2    Hirasawa, M.3    Jacquot, J.P.4    Keryer, E.5    Knaff, D.B.6    Schurmann, P.7
  • 29
    • 77957001732 scopus 로고
    • Reaction of protein sulfhydryl groups with Ellman's reagent
    • Habeeb A.F.S.A. Reaction of protein sulfhydryl groups with Ellman's reagent. Methods Enzymol 1972, 25:457-464.
    • (1972) Methods Enzymol , vol.25 , pp. 457-464
    • Habeeb, A.F.S.A.1
  • 30
    • 1642546383 scopus 로고    scopus 로고
    • Computation and analysis of protein circular dichroism spectra
    • Sreerama N., Woody R.W. Computation and analysis of protein circular dichroism spectra. Methods Enzymol 2004, 383:318-351.
    • (2004) Methods Enzymol , vol.383 , pp. 318-351
    • Sreerama, N.1    Woody, R.W.2
  • 31
    • 0025865875 scopus 로고
    • Substitution of the conserved tryptophan 31 in Escherichia coli thioredoxin by site-directed mutagenesis and structure-function analysis
    • Krause G., Holmgren A. Substitution of the conserved tryptophan 31 in Escherichia coli thioredoxin by site-directed mutagenesis and structure-function analysis. J. Biol. Chem. 1991, 266:4056-4066.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4056-4066
    • Krause, G.1    Holmgren, A.2
  • 32
    • 33645945270 scopus 로고    scopus 로고
    • Properties of the cysteine residues and the iron-sulfur cluster of the assimilatory 5'-adenylyl sulfate reductase from Enteromorpha intestinalis
    • Kim S.K., Rahman A., Conover R.C., Johnson M.K., Mason J.T., Gomes V., Hirasawa M., Moore M.L., Leustek T., Knaff D.B. Properties of the cysteine residues and the iron-sulfur cluster of the assimilatory 5'-adenylyl sulfate reductase from Enteromorpha intestinalis. Biochemistry 2006, 45:5010-5018.
    • (2006) Biochemistry , vol.45 , pp. 5010-5018
    • Kim, S.K.1    Rahman, A.2    Conover, R.C.3    Johnson, M.K.4    Mason, J.T.5    Gomes, V.6    Hirasawa, M.7    Moore, M.L.8    Leustek, T.9    Knaff, D.B.10
  • 33
    • 33751001337 scopus 로고    scopus 로고
    • Thermodynamic basis for redox regulation of the Yap1 signal transduction pathway
    • Mason J.T., Kim S.K., Knaff D.B., Wood M.J. Thermodynamic basis for redox regulation of the Yap1 signal transduction pathway. Biochemistry 2006, 45:13409-13417.
    • (2006) Biochemistry , vol.45 , pp. 13409-13417
    • Mason, J.T.1    Kim, S.K.2    Knaff, D.B.3    Wood, M.J.4
  • 34
    • 33748961329 scopus 로고    scopus 로고
    • Redox properties of the Rhodobacter sphaeroides transcriptional regulatory proteins PpsR and AppA
    • Kim S.K., Mason J.T., Knaff D.B., Bauer C.E., Setterdahl A.T. Redox properties of the Rhodobacter sphaeroides transcriptional regulatory proteins PpsR and AppA. Photosynth. Res. 2006, 89:89-98.
    • (2006) Photosynth. Res. , vol.89 , pp. 89-98
    • Kim, S.K.1    Mason, J.T.2    Knaff, D.B.3    Bauer, C.E.4    Setterdahl, A.T.5
  • 35
    • 0029175398 scopus 로고
    • Measurement of equilibrium midpoint potentials of thiol/disulfide regulatory groups on thioredoxin-activated chloroplast enzymes
    • Hutchison R.S., Ort D.R. Measurement of equilibrium midpoint potentials of thiol/disulfide regulatory groups on thioredoxin-activated chloroplast enzymes. Methods Enzymol 1995, 252:220-228.
    • (1995) Methods Enzymol , vol.252 , pp. 220-228
    • Hutchison, R.S.1    Ort, D.R.2
  • 36
    • 3543029884 scopus 로고    scopus 로고
    • Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS
    • Furukawa Y., Torres A.S., O'Halloran T.V. Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS. EMBO J. 2004, 23:2872-2881.
    • (2004) EMBO J. , vol.23 , pp. 2872-2881
    • Furukawa, Y.1    Torres, A.S.2    O'Halloran, T.V.3
  • 38
    • 0034612325 scopus 로고    scopus 로고
    • Differential effects of chilling-induced photooxidation on the redox regulation of photosynthetic enzymes
    • Hutchison R.S., Groom Q., Ort D.R. Differential effects of chilling-induced photooxidation on the redox regulation of photosynthetic enzymes. Biochemistry 2000, 39:6679-6688.
    • (2000) Biochemistry , vol.39 , pp. 6679-6688
    • Hutchison, R.S.1    Groom, Q.2    Ort, D.R.3
  • 39
    • 33846254144 scopus 로고    scopus 로고
    • The two-domain structure of 5'-adenylylsulfate (APS) reductase from Enteromorpha intestinalis is a requirement for efficient APS reductase activity
    • Kim S.K., Gomes V., Gao Y., Chandramouli K., Johnson M.K., Knaff D.B., Leustek T. The two-domain structure of 5'-adenylylsulfate (APS) reductase from Enteromorpha intestinalis is a requirement for efficient APS reductase activity. Biochemistry 2007, 46:591-601.
    • (2007) Biochemistry , vol.46 , pp. 591-601
    • Kim, S.K.1    Gomes, V.2    Gao, Y.3    Chandramouli, K.4    Johnson, M.K.5    Knaff, D.B.6    Leustek, T.7
  • 41
    • 12144286702 scopus 로고    scopus 로고
    • Cytosolic, mitochondrial thioredoxins and thioredoxin reductases in Arabidopsis thaliana
    • Brehelin C., Laloi C., Setterdahl A.T., Knaff D.B., Meyer Y. Cytosolic, mitochondrial thioredoxins and thioredoxin reductases in Arabidopsis thaliana. Photosynth. Res. 2004, 79:295-304.
    • (2004) Photosynth. Res. , vol.79 , pp. 295-304
    • Brehelin, C.1    Laloi, C.2    Setterdahl, A.T.3    Knaff, D.B.4    Meyer, Y.5
  • 42
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold K., Bordoli L., Kopp J., Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 2006, 22:195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.