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Volumn 10, Issue 5, 2010, Pages 987-1001

Thioredoxin targets of the plant chloroplast lumen and their implications for plastid function

Author keywords

D1 processing; Disulphide; Immunophilin; Pentapeptide protein; Plant proteomics; Violaxanthin de epoxidase

Indexed keywords

TETRAPYRROLE DERIVATIVE; THIOREDOXIN; VIOLAXANTHIN;

EID: 77649126670     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200900654     Document Type: Article
Times cited : (79)

References (78)
  • 1
    • 0036007922 scopus 로고    scopus 로고
    • Central functions of the lumenal and peripheral thylakoid proteome of Arabidopsis determined by experimentation and genome-wide prediction
    • Peltier, J. B., Emanuelsson, O., Kalume, D. E., Ytterberg, J. et al., Central functions of the lumenal and peripheral thylakoid proteome of Arabidopsis determined by experimentation and genome-wide prediction. Plant Cell 2002, 14, 211-236.
    • (2002) Plant Cell , vol.14 , pp. 211-236
    • Peltier, J.B.1    Emanuelsson, O.2    Kalume, D.E.3    Ytterberg, J.4
  • 2
    • 0037040944 scopus 로고    scopus 로고
    • Proteome map of the chloroplast lumen of Arabidopsis thaliana
    • Schubert, M., Petersson, U. A., Haas, B. J., Funk, C. et al., Proteome map of the chloroplast lumen of Arabidopsis thaliana. J. Biol. Chem. 2002, 277, 8354-8365.
    • (2002) J. Biol. Chem , vol.277 , pp. 8354-8365
    • Schubert, M.1    Petersson, U.A.2    Haas, B.J.3    Funk, C.4
  • 3
    • 49249096670 scopus 로고    scopus 로고
    • AtCYP38 ensures early biogenesis, correct assembly and sustenance of photosystem II
    • Sirpiö , S., Khrouchtchova, A., Allahverdiyeva, Y., Hansson, M. et al., AtCYP38 ensures early biogenesis, correct assembly and sustenance of photosystem II. Plant J. 2008, 55, 639-651.
    • (2008) Plant J , vol.55 , pp. 639-651
    • Sirpiö, S.1    Khrouchtchova, A.2    Allahverdiyeva, Y.3    Hansson, M.4
  • 4
    • 35648990552 scopus 로고    scopus 로고
    • A chloroplast cyclophilin functions in the assembly and maintenance of photosystem II in Arabidopsis thaliana
    • Fu, A., He, Z., Sun Cho, H., Lima, A. et al., A chloroplast cyclophilin functions in the assembly and maintenance of photosystem II in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 2007, 104, 15947-15952.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 15947-15952
    • Fu, A.1    He, Z.2    Sun Cho, H.3    Lima, A.4
  • 5
    • 33747584163 scopus 로고    scopus 로고
    • A redox-active FKBP-type immunophilin functions in accumulation of the photosystem II supercomplex in Arabidopsis thaliana
    • Lima, A., Lima, S., Wong, J.H., Phillips, R.S. et al., A redox-active FKBP-type immunophilin functions in accumulation of the photosystem II supercomplex in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 2006, 103, 12631-12636.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 12631-12636
    • Lima, A.1    Lima, S.2    Wong, J.H.3    Phillips, R.S.4
  • 6
    • 33846460028 scopus 로고    scopus 로고
    • The Arabidopsis PsbO2 protein regulates dephosphorylation and turnover of the photosystem II reaction centre D1 protein
    • Lundin, B., Hansson, M., Schoefs, B., Vener, A.V., Spetea, C., The Arabidopsis PsbO2 protein regulates dephosphorylation and turnover of the photosystem II reaction centre D1 protein. Plant J. 2007, 49, 528-539.
    • (2007) Plant J , vol.49 , pp. 528-539
    • Lundin, B.1    Hansson, M.2    Schoefs, B.3    Vener, A.V.4    Spetea, C.5
  • 7
    • 34548787215 scopus 로고    scopus 로고
    • TLP18.3, a novel thylakoid lumen protein regulating photosystem II repair cycle
    • Sirpiö , S., Allahverdiyeva, Y., Suorsa, M., Paakkarinen, V. et al., TLP18.3, a novel thylakoid lumen protein regulating photosystem II repair cycle. Biochem. J. 2007, 406, 415-425.
    • (2007) Biochem. J , vol.406 , pp. 415-425
    • Sirpiö, S.1    Allahverdiyeva, Y.2    Suorsa, M.3    Paakkarinen, V.4
  • 8
    • 1942437977 scopus 로고    scopus 로고
    • Arabidopsis AtCYP20-2 is a light-regulated cyclophilin-type peptidyl-prolyl cis-trans isomerase associated with the photosynthetic membranes
    • Romano, P. G., Edvardsson, A., Ruban, A. V., Andersson, B. et al., Arabidopsis AtCYP20-2 is a light-regulated cyclophilin-type peptidyl-prolyl cis-trans isomerase associated with the photosynthetic membranes. Plant Physiol. 2004, 134, 1244-1247.
    • (2004) Plant Physiol , vol.134 , pp. 1244-1247
    • Romano, P.G.1    Edvardsson, A.2    Ruban, A.V.3    Andersson, B.4
  • 9
    • 67650117729 scopus 로고    scopus 로고
    • AtCYP20-2 is an auxiliary protein of the chloroplast NAD(P)H dehydrogenase complex
    • Sirpiö , S., Holmström, M., Battchikova, N., Aro, E.-M., AtCYP20-2 is an auxiliary protein of the chloroplast NAD(P)H dehydrogenase complex. FEBS Lett. 2009, 583, 2355-2358.
    • (2009) FEBS Lett , vol.583 , pp. 2355-2358
    • Sirpiö, S.1    Holmström, M.2    Battchikova, N.3    Aro, E.-M.4
  • 10
    • 4644251882 scopus 로고    scopus 로고
    • Structural analysis uncovers a role for redox in regulating FKBP13, an immunophilin of the chloroplast thylakoid lumen
    • Gopalan, G., He, Z., Balmer, Y., Romano, P. et al., Structural analysis uncovers a role for redox in regulating FKBP13, an immunophilin of the chloroplast thylakoid lumen. Proc. Natl. Acad. Sci. USA 2004, 101, 13945-13950.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13945-13950
    • Gopalan, G.1    He, Z.2    Balmer, Y.3    Romano, P.4
  • 11
    • 4444327673 scopus 로고    scopus 로고
    • New targets of Arabidopsis thioredoxins revealed by proteomic analysis
    • Marchand, C., Le Marechal, P., Meyer, Y., Migniac-Maslow, M. et al., New targets of Arabidopsis thioredoxins revealed by proteomic analysis. Proteomics 2004, 4, 2696-2706.
    • (2004) Proteomics , vol.4 , pp. 2696-2706
    • Marchand, C.1    Le Marechal, P.2    Meyer, Y.3    Migniac-Maslow, M.4
  • 12
    • 33845968455 scopus 로고    scopus 로고
    • Comparative proteomic approaches for the isolation of proteins interacting with thioredoxin
    • Marchand, C., Le Marechal, P., Meyer, Y., Decottignies, P., Comparative proteomic approaches for the isolation of proteins interacting with thioredoxin. Proteomics 2006, 6, 6528-6537.
    • (2006) Proteomics , vol.6 , pp. 6528-6537
    • Marchand, C.1    Le Marechal, P.2    Meyer, Y.3    Decottignies, P.4
  • 13
    • 0347506349 scopus 로고    scopus 로고
    • The proteome of the chloroplast lumen of higher plants
    • Kieselbach, T., Schröder, W. P., The proteome of the chloroplast lumen of higher plants. Photosynth. Res. 2003, 78, 249-264.
    • (2003) Photosynth. Res , vol.78 , pp. 249-264
    • Kieselbach, T.1    Schröder, W.P.2
  • 14
    • 33750576724 scopus 로고    scopus 로고
    • The Prx Q protein of Arabidopsis thaliana is a member of the lumenal chloroplast proteome
    • Petersson, U., Kieselbach, T., García-Cerdán, J. G., Schröder, W. P., The Prx Q protein of Arabidopsis thaliana is a member of the lumenal chloroplast proteome. FEBS Lett. 2006, 580, 6055-6061.
    • (2006) FEBS Lett , vol.580 , pp. 6055-6061
    • Petersson, U.1    Kieselbach, T.2    García-Cerdán, J.G.3    Schröder, W.P.4
  • 15
    • 33644753761 scopus 로고    scopus 로고
    • Peroxiredoxin Q of Arabidopsis thaliana is attached to the thylakoids and functions in the context of photosynthesis
    • Lamkemeyer, P., Laxa, M., Collin, V., Li, W. et al., Peroxiredoxin Q of Arabidopsis thaliana is attached to the thylakoids and functions in the context of photosynthesis. Plant J. 2006, 45, 968-981.
    • (2006) Plant J , vol.45 , pp. 968-981
    • Lamkemeyer, P.1    Laxa, M.2    Collin, V.3    Li, W.4
  • 16
    • 33745617040 scopus 로고    scopus 로고
    • The functions of peroxiredoxins in plant organelle redox metabolism
    • Dietz, K.-J., Jacob, S., Oelze, M. L., Laxa, M. et al., The functions of peroxiredoxins in plant organelle redox metabolism. J. Exp. Bot. 2006, 57, 1697-1709.
    • (2006) J. Exp. Bot , vol.57 , pp. 1697-1709
    • Dietz, K.-J.1    Jacob, S.2    Oelze, M.L.3    Laxa, M.4
  • 18
    • 0035209897 scopus 로고    scopus 로고
    • HCF164 encodes a thioredoxin-like protein involved in the biogenesis of the cytochrome b(6)f complex in Arabidopsis
    • Lennartz, K., Pl . ucken, H., Seidler, A., Westhoff, P. et al., HCF164 encodes a thioredoxin-like protein involved in the biogenesis of the cytochrome b(6)f complex in Arabidopsis. Plant Cell 2001, 13, 2539-2551.
    • (2001) Plant Cell , vol.13 , pp. 2539-2551
    • Lennartz, K.1    Pl2    ucken, H.3    Seidler, A.4    Westhoff, P.5
  • 19
    • 4544258776 scopus 로고    scopus 로고
    • The unusual transmembrane electron transporter DsbD and its homologues: A bacterial family of disulfide reductases
    • Porat, A., Cho, S. H., Beckwith, J., The unusual transmembrane electron transporter DsbD and its homologues: a bacterial family of disulfide reductases. Res. Microbiol. 2004, 155, 617-622.
    • (2004) Res. Microbiol , vol.155 , pp. 617-622
    • Porat, A.1    Cho, S.H.2    Beckwith, J.3
  • 20
    • 33845939598 scopus 로고    scopus 로고
    • HCF164 receives reducing equivalents from stromal thioredoxin across the thylakoid membrane and mediates reduction of target proteins in the thylakoid lumen
    • Motohashi, K., Hisabori, T., HCF164 receives reducing equivalents from stromal thioredoxin across the thylakoid membrane and mediates reduction of target proteins in the thylakoid lumen. J. Biol. Chem. 2006, 281, 35039-35047.
    • (2006) J. Biol. Chem , vol.281 , pp. 35039-35047
    • Motohashi, K.1    Hisabori, T.2
  • 21
    • 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
  • 23
    • 63349083179 scopus 로고    scopus 로고
    • Disulphide proteomes and interactions with thioredoxin on the track towards understanding redox regulation in chloroplasts and cyanobacteria
    • Lindahl, M., Kieselbach, T., Disulphide proteomes and interactions with thioredoxin on the track towards understanding redox regulation in chloroplasts and cyanobacteria. J. Proteomics 2009, 72, 416-438.
    • (2009) J. Proteomics , vol.72 , pp. 416-438
    • Lindahl, M.1    Kieselbach, T.2
  • 24
    • 41449117607 scopus 로고    scopus 로고
    • Thioredoxins and glutaredoxins as facilitators of protein folding
    • Berndt, C., Lillig, C. H., Holmgren, A., Thioredoxins and glutaredoxins as facilitators of protein folding. Biochim. Biophys. Acta 2008, 1783, 641-650.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 641-650
    • Berndt, C.1    Lillig, C.H.2    Holmgren, A.3
  • 25
    • 0035836648 scopus 로고    scopus 로고
    • A stra tegy for the identification of proteins targeted by thioredoxin
    • Yano, H., Wong, J. H., Lee, Y. M., Buchanan, B. B., A stra tegy for the identification of proteins targeted by thioredoxin. Proc. Natl. Acad. Sci. USA 2001, 98, 4794-4799.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4794-4799
    • Yano, H.1    Wong, J.H.2    Lee, Y.M.3    Buchanan, B.B.4
  • 26
    • 3242791842 scopus 로고    scopus 로고
    • Thioredoxin targets of developing wheat seeds identified by complementary proteomic approaches
    • Wong, J. H., Cai, N., Balmer, Y., Tanaka, C. K. et al., Thioredoxin targets of developing wheat seeds identified by complementary proteomic approaches. Phytochemistry 2004, 65, 1629-1640.
    • (2004) Phytochemistry , vol.65 , pp. 1629-1640
    • Wong, J.H.1    Cai, N.2    Balmer, Y.3    Tanaka, C.K.4
  • 27
  • 28
    • 0037422610 scopus 로고    scopus 로고
    • Proteomics gives insight into the regulatory function of chloroplast thioredoxins
    • Balmer, Y., Koller, A., del Val, G., Manieri, W. et al., Proteomics gives insight into the regulatory function of chloroplast thioredoxins. Proc. Natl. Acad. Sci. USA 2003, 100, 370-375.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 370-375
    • Balmer, Y.1    Koller, A.2    del Val, G.3    Manieri, W.4
  • 29
    • 4344677972 scopus 로고    scopus 로고
    • Determining cysteine oxidation status using differential alkylation
    • Schilling, B., Yoo, C. B., Collins, C. J., Gibson, B. W., Determining cysteine oxidation status using differential alkylation. Int. J. Mass Spectrom. 2004, 236, 117-127.
    • (2004) Int. J. Mass Spectrom , vol.236 , pp. 117-127
    • Schilling, B.1    Yoo, C.B.2    Collins, C.J.3    Gibson, B.W.4
  • 30
    • 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
  • 31
    • 0037628370 scopus 로고    scopus 로고
    • Unraveling thioredoxin-linked metabolic processes of cereal starchy endosperm using proteomics
    • Wong, J. H., Balmer, Y., Cai, N., Tanaka, C. K. et al., Unraveling thioredoxin-linked metabolic processes of cereal starchy endosperm using proteomics. FEBS Lett. 2003, 547, 151-156.
    • (2003) FEBS Lett , vol.547 , pp. 151-156
    • Wong, J.H.1    Balmer, Y.2    Cai, N.3    Tanaka, C.K.4
  • 32
    • 0346103649 scopus 로고    scopus 로고
    • Thioredoxin-linked processes in cyanobacteria are as numerous as in chloroplasts, but targets are different
    • Lindahl, M., Florencio, F. J., Thioredoxin-linked processes in cyanobacteria are as numerous as in chloroplasts, but targets are different. Proc. Natl. Acad. Sci. USA 2003, 100, 16107-16112.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 16107-16112
    • Lindahl, M.1    Florencio, F.J.2
  • 33
    • 1242271986 scopus 로고    scopus 로고
    • Systematic screening of reactive cysteine proteomes
    • Lindahl, M., Florencio, F. J., Systematic screening of reactive cysteine proteomes. Proteomics 2004, 4, 448-450.
    • (2004) Proteomics , vol.4 , pp. 448-450
    • Lindahl, M.1    Florencio, F.J.2
  • 35
    • 36048943681 scopus 로고    scopus 로고
    • Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin
    • Mata-Cabana, A., Florencio, F. J., Lindahl, M., Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin. Proteomics 2007, 7, 3953-3963.
    • (2007) Proteomics , vol.7 , pp. 3953-3963
    • Mata-Cabana, A.1    Florencio, F.J.2    Lindahl, M.3
  • 36
    • 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
  • 37
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T., Gordon, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 1979, 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 38
    • 34548103850 scopus 로고    scopus 로고
    • Immunophilin AtFKBP13 sustains all peptidyl-prolyl isomerase activity in the thylakoid lumen from Arabidopsis thaliana deficient in AtCYP20-2
    • Edvardsson, A., Shapiguzov, A., Petersson, U. A., Schröder, W. P., Vener, A. V., Immunophilin AtFKBP13 sustains all peptidyl-prolyl isomerase activity in the thylakoid lumen from Arabidopsis thaliana deficient in AtCYP20-2. Biochemistry 2007, 46, 9432-9442.
    • (2007) Biochemistry , vol.46 , pp. 9432-9442
    • Edvardsson, A.1    Shapiguzov, A.2    Petersson, U.A.3    Schröder, W.P.4    Vener, A.V.5
  • 39
    • 33847001993 scopus 로고    scopus 로고
    • Localization of the small CAB-like proteins in photosystem II
    • Yao, D., Kieselbach, T., Komenda, J., Promnares, K. et al., Localization of the small CAB-like proteins in photosystem II. J. Biol. Chem. 2007, 282, 267-276.
    • (2007) J. Biol. Chem , vol.282 , pp. 267-276
    • Yao, D.1    Kieselbach, T.2    Komenda, J.3    Promnares, K.4
  • 40
    • 34249826038 scopus 로고    scopus 로고
    • Purification of a plant mediator from Arabidopsis thaliana identifies PFT1 as the Med25 subunit
    • Bäckström, S., Elfving, N., Nilsson, R., Wingsle, G., Björklund, S., Purification of a plant mediator from Arabidopsis thaliana identifies PFT1 as the Med25 subunit. Mol. Cell 2007, 26, 717-729.
    • (2007) Mol. Cell , vol.26 , pp. 717-729
    • Bäckström, S.1    Elfving, N.2    Nilsson, R.3    Wingsle, G.4    Björklund, S.5
  • 41
    • 37749002134 scopus 로고    scopus 로고
    • Association of small CAB-like proteins (SCPs) of Synechocystis sp. PCC 6803 with photosystem II
    • Kufryk, G., Hernandez-Prieto, M.A., Kieselbach, T., Miranda, H. et al., Association of small CAB-like proteins (SCPs) of Synechocystis sp. PCC 6803 with photosystem II. Photosynth. Res. 2008, 95, 135-145.
    • (2008) Photosynth. Res , vol.95 , pp. 135-145
    • Kufryk, G.1    Hernandez-Prieto, M.A.2    Kieselbach, T.3    Miranda, H.4
  • 42
    • 7444220226 scopus 로고    scopus 로고
    • Role of histidines in the binding of violaxanthin de-epoxidase to the thylakoid membrane as studied by site directed mutagenesis
    • Gisselsson, A., Szilágyi, A., Åkerlund, H.-E., Role of histidines in the binding of violaxanthin de-epoxidase to the thylakoid membrane as studied by site directed mutagenesis. Physiol. Plant. 2004, 122, 337-343.
    • (2004) Physiol. Plant , vol.122 , pp. 337-343
    • Gisselsson, A.1    Szilágyi, A.2    Åkerlund, H.-E.3
  • 43
    • 0018129919 scopus 로고
    • Violaxanthin de-epoxidase-lipid composition and substrate specificity
    • Yamamoto, H. Y., Higashi, R. M., Violaxanthin de-epoxidase-lipid composition and substrate specificity. Arch. Biochem. Biophys. 1978, 190, 514-522.
    • (1978) Arch. Biochem. Biophys , vol.190 , pp. 514-522
    • Yamamoto, H.Y.1    Higashi, R.M.2
  • 44
    • 0000700968 scopus 로고
    • Evidence for an active-center histidine in trypsin through use of a specific reagent, 1-chloro-3-tosylamido-7- amino-2-heptanon, the chloromethyl ketone derived from Nα-tosyl-L-lysine
    • Shaw, E., Mares-Guia, M., Cohen, W., Evidence for an active-center histidine in trypsin through use of a specific reagent, 1-chloro-3-tosylamido-7- amino-2-heptanon, the chloromethyl ketone derived from Nα-tosyl-L-lysine. Biochemistry 1965, 10, 2219-2224.
    • (1965) Biochemistry , vol.10 , pp. 2219-2224
    • Shaw, E.1    Mares-Guia, M.2    Cohen, W.3
  • 45
    • 0009738251 scopus 로고
    • The identification of the histidine residue at the active center of chymotrypsin
    • Ong, E. B., Shaw, E., Schoellmann, G., The identification of the histidine residue at the active center of chymotrypsin. J. Biol. Chem. 1965, 240, 694-698.
    • (1965) J. Biol. Chem , vol.240 , pp. 694-698
    • Ong, E.B.1    Shaw, E.2    Schoellmann, G.3
  • 46
    • 33748980307 scopus 로고    scopus 로고
    • Selecting thioredoxins for disulphide proteomics: Target proteomes of three thioredoxins from the cyanobacterium Synechocystis sp. PCC 6803
    • Pérez-Pérez, M. E., Florencio, F. J., Lindahl, M., Selecting thioredoxins for disulphide proteomics: target proteomes of three thioredoxins from the cyanobacterium Synechocystis sp. PCC 6803. Proteomics 2006, 6, S186-S195.
    • (2006) Proteomics , vol.6
    • Pérez-Pérez, M.E.1    Florencio, F.J.2    Lindahl, M.3
  • 48
    • 2442498463 scopus 로고    scopus 로고
    • New thioredoxin targets in the unicellular photosynthetic eukaryote Chlamydomonas reinhardtii
    • Lemaire, S. D., Guillon, B., Le Marechál, P., Keryer, E. et al., New thioredoxin targets in the unicellular photosynthetic eukaryote Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA 2004, 101, 7475-7480.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7475-7480
    • Lemaire, S.D.1    Guillon, B.2    Le Marechál, P.3    Keryer, E.4
  • 49
    • 34249874824 scopus 로고    scopus 로고
    • Thioredoxins, glutaredoxins, and glutathionylation: New crosstalks to explore
    • Michelet, L., Zaffagnini, M., Massot, V., Keryer, E. et al., Thioredoxins, glutaredoxins, and glutathionylation: new crosstalks to explore. Photosynth. Res. 2006, 89, 225-245.
    • (2006) Photosynth. Res , vol.89 , pp. 225-245
    • Michelet, L.1    Zaffagnini, M.2    Massot, V.3    Keryer, E.4
  • 50
    • 57649233549 scopus 로고    scopus 로고
    • Mechanism and regulation of the violaxanthin cycle: The role of antenna proteins and membrane lipids
    • Jahns, P., Latowski, D., Strzalka, K., Mechanism and regulation of the violaxanthin cycle: The role of antenna proteins and membrane lipids. Biochim. Biophys. Acta 2009, 1787, 3-14.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 3-14
    • Jahns, P.1    Latowski, D.2    Strzalka, K.3
  • 51
    • 0015520731 scopus 로고
    • The effects of dithiothreitol on violaxanthin de-epoxidation and absorbance changes in the 500-nm region
    • Yamamoto, H. Y., Kamite, L., The effects of dithiothreitol on violaxanthin de-epoxidation and absorbance changes in the 500-nm region. Biochem. Biophys. Acta 1972, 267, 538-543.
    • (1972) Biochem. Biophys. Acta , vol.267 , pp. 538-543
    • Yamamoto, H.Y.1    Kamite, L.2
  • 52
    • 0017232307 scopus 로고
    • Ascorbate-independent carotenoids de-epoxidation in intact chloroplasts
    • Sokolove, P. M., Marsho, T. V., Ascorbate-independent carotenoids de-epoxidation in intact chloroplasts. Biochem. Biophys. Acta 1976, 430, 321-326.
    • (1976) Biochem. Biophys. Acta , vol.430 , pp. 321-326
    • Sokolove, P.M.1    Marsho, T.V.2
  • 53
    • 36849027691 scopus 로고    scopus 로고
    • Both the stroma and thylakoid lumen of tobacco chloroplasts are competent for the formation of disulphide bonds in recombinant proteins
    • Bally, J., Paget, E., Droux, M., Job, C. et al., Both the stroma and thylakoid lumen of tobacco chloroplasts are competent for the formation of disulphide bonds in recombinant proteins. Plant Biotechnol. J. 2008, 6, 46-61.
    • (2008) Plant Biotechnol. J , vol.6 , pp. 46-61
    • Bally, J.1    Paget, E.2    Droux, M.3    Job, C.4
  • 54
    • 40349091373 scopus 로고    scopus 로고
    • Translocation of aprotinin, a therapeutic protease inhibitor, into the thylakoid lumen of genetically engineered tobacco chloroplasts
    • Tissot, G., Canard, H., Nadai, A., Martone, A. et al., Translocation of aprotinin, a therapeutic protease inhibitor, into the thylakoid lumen of genetically engineered tobacco chloroplasts. Plant Biotechnol. J. 2008, 6, 309-320.
    • (2008) Plant Biotechnol. J , vol.6 , pp. 309-320
    • Tissot, G.1    Canard, H.2    Nadai, A.3    Martone, A.4
  • 55
    • 33745173773 scopus 로고    scopus 로고
    • Profound redox sensitivity of peptidyl-prolyl isomerase activity in Arabidopsis thylakoid lumen
    • Shapiguzov, A., Edvardsson, A., Vener, A. V., Profound redox sensitivity of peptidyl-prolyl isomerase activity in Arabidopsis thylakoid lumen. FEBS Lett. 2006, 580, 3671-3676.
    • (2006) FEBS Lett , vol.580 , pp. 3671-3676
    • Shapiguzov, A.1    Edvardsson, A.2    Vener, A.V.3
  • 56
    • 18344416024 scopus 로고    scopus 로고
    • A chloroplast FKBP interacts with and affects the accumulation of Rieske subunit of cytochrome bf complex
    • Gupta, R., Mould, R. M., He, Z., Luan, S., A chloroplast FKBP interacts with and affects the accumulation of Rieske subunit of cytochrome bf complex. Proc. Natl. Acad. Sci. USA 2002, 99, 15806-15811.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15806-15811
    • Gupta, R.1    Mould, R.M.2    He, Z.3    Luan, S.4
  • 57
    • 0032536779 scopus 로고    scopus 로고
    • A novel multi-functional chloroplast protein: Identification of a 40 kDa immunophilin-like protein located in the thylakoid lumen
    • Fulgosi, H., Vener, A. V., Altschmied, L., Herrmann, R. G., Andersson, B., A novel multi-functional chloroplast protein: identification of a 40 kDa immunophilin-like protein located in the thylakoid lumen. EMBO J. 1998, 17, 1577-1587.
    • (1998) EMBO J , vol.17 , pp. 1577-1587
    • Fulgosi, H.1    Vener, A.V.2    Altschmied, L.3    Herrmann, R.G.4    Andersson, B.5
  • 58
    • 0032549515 scopus 로고    scopus 로고
    • The thylakoid lumen of chloroplasts. Isolation and characterization
    • Kieselbach, T., Hagman, Å., Andersson, B., Schröder, W. P., The thylakoid lumen of chloroplasts. Isolation and characterization. J. Biol. Chem. 1998, 273, 6710-6716.
    • (1998) J. Biol. Chem , vol.273 , pp. 6710-6716
    • Kieselbach, T.1    Hagman, A.2    Andersson, B.3    Schröder, W.P.4
  • 59
    • 10944243117 scopus 로고    scopus 로고
    • Proteolysis as a regulatory mechanism
    • Ehrmann, M., Clausen, T., Proteolysis as a regulatory mechanism. Annu. Rev. Genet. 2004, 38, 709-724.
    • (2004) Annu. Rev. Genet , vol.38 , pp. 709-724
    • Ehrmann, M.1    Clausen, T.2
  • 60
    • 57849108459 scopus 로고    scopus 로고
    • PsbO of photosystem II: Overexpression in Escherichia coli and the importance of a single disulfide bond for the protein structure stability
    • Nikitina, J., Shutova, T., Melnik, B., Chernyshev, S. et al., PsbO of photosystem II: overexpression in Escherichia coli and the importance of a single disulfide bond for the protein structure stability. Photosynth. Res. 2008, 98, 391-403.
    • (2008) Photosynth. Res , vol.98 , pp. 391-403
    • Nikitina, J.1    Shutova, T.2    Melnik, B.3    Chernyshev, S.4
  • 61
    • 33751082083 scopus 로고    scopus 로고
    • Structural comparison of oxidized and reduced FKBP13 from Arabidopsis thaliana
    • Gopalan, G., He, Z., Battaile, K. P., Luan, S., Swaminathan, K., Structural comparison of oxidized and reduced FKBP13 from Arabidopsis thaliana. Proteins 2006, 65, 789-795.
    • (2006) Proteins , vol.65 , pp. 789-795
    • Gopalan, G.1    He, Z.2    Battaile, K.P.3    Luan, S.4    Swaminathan, K.5
  • 62
    • 0033048929 scopus 로고    scopus 로고
    • Thioredoxin treatment increases digestibility and lowers allergenicity of milk
    • del Val, G., Yee, B. C., Lozano, R. M., Buchanan, B. B. et al., Thioredoxin treatment increases digestibility and lowers allergenicity of milk. J. Allergy Clin. Immunol. 1999, 103, 690-697.
    • (1999) J. Allergy Clin. Immunol , vol.103 , pp. 690-697
    • del Val, G.1    Yee, B.C.2    Lozano, R.M.3    Buchanan, B.B.4
  • 63
    • 0000579043 scopus 로고
    • Effect of thioredoxin-linked reduction on the activity and stability of the Kunitz and Bowman-birk soybean trypsin inhibitor proteins
    • Jiao, J., Yee, B. C., Kobrehel, K., Buchanan, B. B., Effect of thioredoxin-linked reduction on the activity and stability of the Kunitz and Bowman-birk soybean trypsin inhibitor proteins. J. Agric. Food Chem. 1992, 40, 2333-2338.
    • (1992) J. Agric. Food Chem , vol.40 , pp. 2333-2338
    • Jiao, J.1    Yee, B.C.2    Kobrehel, K.3    Buchanan, B.B.4
  • 64
    • 0242277339 scopus 로고    scopus 로고
    • The family of Deg/HtrA proteases: From Escherichia coli to Arabidopsis
    • Kieselbach, T., Funk, C., The family of Deg/HtrA proteases: from Escherichia coli to Arabidopsis. Physiol. Plant. 2003, 119, 337-346.
    • (2003) Physiol. Plant , vol.119 , pp. 337-346
    • Kieselbach, T.1    Funk, C.2
  • 65
    • 34250636225 scopus 로고    scopus 로고
    • Formation of DEG5 and DEG8 complexes and their involvement in the degradation of photodamaged photosystem II reaction center D1 protein in Arabidopsis
    • Sun, X., Peng, L., Guo, J., Chi, W. et al., Formation of DEG5 and DEG8 complexes and their involvement in the degradation of photodamaged photosystem II reaction center D1 protein in Arabidopsis. Plant Cell 2007, 19, 1347-1361.
    • (2007) Plant Cell , vol.19 , pp. 1347-1361
    • Sun, X.1    Peng, L.2    Guo, J.3    Chi, W.4
  • 66
    • 34250613221 scopus 로고    scopus 로고
    • The thylakoid lumen protease Deg1 is involved in the repair of photosystem II from photoinhibition in Arabidopsis
    • Kapri-Pardes, E., Naveh, L., Adam, Z., The thylakoid lumen protease Deg1 is involved in the repair of photosystem II from photoinhibition in Arabidopsis. Plant Cell 2007, 19, 1039-1047.
    • (2007) Plant Cell , vol.19 , pp. 1039-1047
    • Kapri-Pardes, E.1    Naveh, L.2    Adam, Z.3
  • 67
    • 45249097787 scopus 로고    scopus 로고
    • The dynamic thiol-disulphide redox proteome of the Arabidopsis thaliana chloroplast as revealed by differential electrophoretic mobility
    • Ströher, E., Dietz, K.-J., The dynamic thiol-disulphide redox proteome of the Arabidopsis thaliana chloroplast as revealed by differential electrophoretic mobility. Physiol. Plant. 2008, 133, 566-583.
    • (2008) Physiol. Plant , vol.133 , pp. 566-583
    • Ströher, E.1    Dietz, K.-J.2
  • 68
    • 0033791940 scopus 로고    scopus 로고
    • Biogenesis of the chloroplast-encoded D1 protein regulation of translation elongation, insertion and assembly into photosystem II
    • Zhang, L., Paakkarinen, V., van Wijk, K. J., Aro, E. M., Biogenesis of the chloroplast-encoded D1 protein regulation of translation elongation, insertion and assembly into photosystem II. Plant Cell 2000, 12, 1769-1782.
    • (2000) Plant Cell , vol.12 , pp. 1769-1782
    • Zhang, L.1    Paakkarinen, V.2    van Wijk, K.J.3    Aro, E.M.4
  • 69
    • 42949151399 scopus 로고    scopus 로고
    • The ferredoxin/thioredoxin of oxygenic photosynthesis
    • Schürmann, P., Buchanan, B. B., The ferredoxin/thioredoxin of oxygenic photosynthesis. Antioxid. Redox Signal. 2008, 10, 1235-1274.
    • (2008) Antioxid. Redox Signal , vol.10 , pp. 1235-1274
    • Schürmann, P.1    Buchanan, B.B.2
  • 70
    • 20044395966 scopus 로고    scopus 로고
    • Redox regulation in the chloroplast thylakoid lumen: A new frontier in photosynthesis research
    • Buchanan, B. B., Luan, S., Redox regulation in the chloroplast thylakoid lumen: a new frontier in photosynthesis research. J. Exp. Bot. 2005, 56, 1439-1447.
    • (2005) J. Exp. Bot , vol.56 , pp. 1439-1447
    • Buchanan, B.B.1    Luan, S.2
  • 71
    • 47049096139 scopus 로고    scopus 로고
    • Identification of an atypical membrane protein involved in the formation of protein disulfide bonds in oxygenic photosynthetic organisms
    • Singh, A.K., Bhattacharyya-Pakrasi, M., Pakrasi, H. B., Identification of an atypical membrane protein involved in the formation of protein disulfide bonds in oxygenic photosynthetic organisms. J. Biol. Chem. 2008, 283, 15762-15770.
    • (2008) J. Biol. Chem , vol.283 , pp. 15762-15770
    • Singh, A.K.1    Bhattacharyya-Pakrasi, M.2    Pakrasi, H.B.3
  • 76
    • 0034144398 scopus 로고    scopus 로고
    • Distinguishing between luminal and localized proton buffering pools in thylakoid membranes
    • Ewy, R. G., Dilley, R. A., Distinguishing between luminal and localized proton buffering pools in thylakoid membranes. Plant Physiol. 2000, 122, 583-595.
    • (2000) Plant Physiol , vol.122 , pp. 583-595
    • Ewy, R.G.1    Dilley, R.A.2
  • 77
    • 33749233825 scopus 로고    scopus 로고
    • Rice NTRC is a high-efficiency redox system for chloroplast protection against oxidative damage
    • Pérez-Ruiz, J. M., Spínola, M. C., Kirchsteiger, K., Moreno, J. et al., Rice NTRC is a high-efficiency redox system for chloroplast protection against oxidative damage. Plant Cell 2006, 18, 2356-2368.
    • (2006) Plant Cell , vol.18 , pp. 2356-2368
    • Pérez-Ruiz, J.M.1    Spínola, M.C.2    Kirchsteiger, K.3    Moreno, J.4


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