메뉴 건너뛰기




Volumn 89, Issue 2, 2006, Pages 157-171

The diversity and complexity of the cyanobacterial thioredoxin systems

Author keywords

Cyanobacteria; Genome; Synechocystis; Thioredoxin

Indexed keywords

FUNGAL PROTEIN; THIOREDOXIN;

EID: 33748959014     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11120-006-9093-5     Document Type: Review
Times cited : (69)

References (66)
  • 1
    • 0024486565 scopus 로고
    • Isolation, sequence, and expression in Escherichia coli of an unusual thioredoxin gene from the cyanobacterium Anabaena sp. strain PCC 7120
    • Alam J, Curtis S, Gleason FK, Gerami-Nejad M, Fuchs JA (1989) Isolation, sequence, and expression in Escherichia coli of an unusual thioredoxin gene from the cyanobacterium Anabaena sp. strain PCC 7120. J Bacteriol 171:162-171
    • (1989) J Bacteriol , vol.171 , pp. 162-171
    • Alam, J.1    Curtis, S.2    Gleason, F.K.3    Gerami-Nejad, M.4    Fuchs, J.A.5
  • 5
    • 0030043399 scopus 로고    scopus 로고
    • The molecular pathway for the regulation of phosphoribulokinase by thioredoxin f
    • Brandes HK, Larimer FW, Hartman FC (1996) The molecular pathway for the regulation of phosphoribulokinase by thioredoxin f. J Biol Chem 271:3333-3335
    • (1996) J Biol Chem , vol.271 , pp. 3333-3335
    • Brandes, H.K.1    Larimer, F.W.2    Hartman, F.C.3
  • 6
    • 0000765807 scopus 로고
    • Role of light in the regulation of chloroplast enzymes
    • Buchanan BB (1980) Role of light in the regulation of chloroplast enzymes. Annu Rev Plant Physiol 31:341-374
    • (1980) Annu Rev Plant Physiol , vol.31 , pp. 341-374
    • Buchanan, B.B.1
  • 7
    • 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
  • 8
    • 0036413565 scopus 로고    scopus 로고
    • The ferredoxin/thioredoxin system: From discovery to molecular structures and beyond
    • Buchanan BB, Schurmann P, Wolosiuk RA, Jacquot JP (2002) The ferredoxin/thioredoxin system: from discovery to molecular structures and beyond. Photosynth Res 73:215-222
    • (2002) Photosynth Res , vol.73 , pp. 215-222
    • Buchanan, B.B.1    Schurmann, P.2    Wolosiuk, R.A.3    Jacquot, J.P.4
  • 9
    • 28044436397 scopus 로고    scopus 로고
    • Accelerated evolution associated with genome reduction in a free-living prokaryote
    • Dufresne A, Garczarek L, Partensky F (2005) Accelerated evolution associated with genome reduction in a free-living prokaryote. Genome Biol 6:R14
    • (2005) Genome Biol , vol.6
    • Dufresne, A.1    Garczarek, L.2    Partensky, F.3
  • 10
    • 0024110181 scopus 로고
    • An NADP/thioredoxin system in leaves: Purification and characterization of NADP-thioredoxin reductase and thioredoxin h from spinach
    • Florencio FJ, Yee BC, Johnson TC, Buchanan BB (1988) An NADP/thioredoxin system in leaves: purification and characterization of NADP-thioredoxin reductase and thioredoxin h from spinach. Arch Biochem Biophys 266:496-507
    • (1988) Arch Biochem Biophys , vol.266 , pp. 496-507
    • Florencio, F.J.1    Yee, B.C.2    Johnson, T.C.3    Buchanan, B.B.4
  • 11
    • 10344237544 scopus 로고    scopus 로고
    • Streamlined regulation and gene loss as adaptive mechanisms in Prochlorococcus for optimized nitrogen utilization in oligotrophic environments
    • Garcia-Fernandez JM, de Marsac NT, Diez J (2004) Streamlined regulation and gene loss as adaptive mechanisms in Prochlorococcus for optimized nitrogen utilization in oligotrophic environments. Microbiol Mol Biol Rev 68:630-638
    • (2004) Microbiol Mol Biol Rev , vol.68 , pp. 630-638
    • Garcia-Fernandez, J.M.1    De Marsac, N.T.2    Diez, J.3
  • 12
    • 0030588315 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase from the cyanobacterium, Anabaena sp. PCC 7120: Purification and kinetics of redox modulation
    • Gleason FK (1996) Glucose-6-phosphate dehydrogenase from the cyanobacterium, Anabaena sp. PCC 7120: purification and kinetics of redox modulation. Arch Biochem Biophys 334:277-283
    • (1996) Arch Biochem Biophys , vol.334 , pp. 277-283
    • Gleason, F.K.1
  • 13
    • 0019888353 scopus 로고
    • Isolation and characterization of thioredoxin from the cyanobacterium, Anabaena sp.
    • Gleason FK, Holmgren A (1981) Isolation and characterization of thioredoxin from the cyanobacterium, Anabaena sp. J Biol Chem 256:8306-8309
    • (1981) J Biol Chem , vol.256 , pp. 8306-8309
    • Gleason, F.K.1    Holmgren, A.2
  • 14
    • 0024147201 scopus 로고
    • Thioredoxin and related proteins in prokaryotes
    • Gleason FK, Holmgren A (1988) Thioredoxin and related proteins in prokaryotes. FEMS Microbiol Rev 4:271-297
    • (1988) FEMS Microbiol Rev , vol.4 , pp. 271-297
    • Gleason, F.K.1    Holmgren, A.2
  • 15
    • 0000962563 scopus 로고
    • Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution
    • Holmgren A, Soderberg BO, Eklund H, Branden CI (1975) Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution. Proc Natl Acad Sci USA 72:2305-2309
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 2305-2309
    • Holmgren, A.1    Soderberg, B.O.2    Eklund, H.3    Branden, C.I.4
  • 16
    • 12844253100 scopus 로고    scopus 로고
    • Anti-oxidative stress system in cyanobacteria. Significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803
    • Hosoya-Matsuda N, Motohashi K, Yoshimura H, Nozaki A, Inoue K, Ohmori M, Hisabori T (2005) Anti-oxidative stress system in cyanobacteria. Significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803. J Biol Chem 280:840-846
    • (2005) J Biol Chem , vol.280 , pp. 840-846
    • Hosoya-Matsuda, N.1    Motohashi, K.2    Yoshimura, H.3    Nozaki, A.4    Inoue, K.5    Ohmori, M.6    Hisabori, T.7
  • 17
    • 0031444519 scopus 로고    scopus 로고
    • Thioredoxins: Structure and function in plant cells
    • Jacquot JP, Lancelin JM, Meyer Y (1997) Thioredoxins: structure and function in plant cells. New Phytol 136:543-570
    • (1997) New Phytol , vol.136 , pp. 543-570
    • Jacquot, J.P.1    Lancelin, J.M.2    Meyer, Y.3
  • 18
    • 0037257313 scopus 로고    scopus 로고
    • An unusual phylogenetic variation in the metal ion binding sites of porphobilinogen synthase
    • Jaffe EK (2003) An unusual phylogenetic variation in the metal ion binding sites of porphobilinogen synthase. Chem Biol 10:25-34
    • (2003) Chem Biol , vol.10 , pp. 25-34
    • Jaffe, E.K.1
  • 21
    • 0345382697 scopus 로고    scopus 로고
    • Molecular characterization and redox regulation of phosphoribulokinase from the cyanobacterium Synechococcus sp. PCC 7942
    • Kobayashi D, Tamoi M, Iwaki T, Shigeoka S, Wadano A (2003) Molecular characterization and redox regulation of phosphoribulokinase from the cyanobacterium Synechococcus sp. PCC 7942. Plant Cell Physiol 44:269-276
    • (2003) Plant Cell Physiol , vol.44 , pp. 269-276
    • Kobayashi, D.1    Tamoi, M.2    Iwaki, T.3    Shigeoka, S.4    Wadano, A.5
  • 22
    • 0028829386 scopus 로고
    • ATP synthase from a cyanobacterial Synechocystis 6803 mutant containing the regulatory segment of the chloroplast gamma subunit shows thiol modulation
    • Krenn BE, Aardewijn P, Van Walraven HS, Werner-Grune S, Strotmann H, Kraayenhof R (1995) ATP synthase from a cyanobacterial Synechocystis 6803 mutant containing the regulatory segment of the chloroplast gamma subunit shows thiol modulation. Biochem Soc Trans 23:757-760
    • (1995) Biochem Soc Trans , vol.23 , pp. 757-760
    • Krenn, B.E.1    Aardewijn, P.2    Van Walraven, H.S.3    Werner-Grune, S.4    Strotmann, H.5    Kraayenhof, R.6
  • 24
    • 0038393110 scopus 로고    scopus 로고
    • Characterization of thioredoxin y, a new type of thioredoxin identified in the genome of Chlamydomonas reinhardtii
    • Lemaire SD, Collin V, Keryer E, Quesada A, Miginiac-Maslow M (2003) Characterization of thioredoxin y, a new type of thioredoxin identified in the genome of Chlamydomonas reinhardtii. FEBS Lett 543:87-92
    • (2003) FEBS Lett , vol.543 , pp. 87-92
    • Lemaire, S.D.1    Collin, V.2    Keryer, E.3    Quesada, A.4    Miginiac-Maslow, M.5
  • 26
    • 0020825806 scopus 로고
    • Molecular properties of 5-aminolevulinic acid dehydratase from Spinacia oleracea
    • Liedgens W, Lutz C, Schneider HA (1983) Molecular properties of 5-aminolevulinic acid dehydratase from Spinacia oleracea. Eur J Biochem 135:75-79
    • (1983) Eur J Biochem , vol.135 , pp. 75-79
    • Liedgens, W.1    Lutz, C.2    Schneider, H.A.3
  • 27
    • 0022908613 scopus 로고
    • Cloning, expression, and characterization of the Anabaena thioredoxin gene in Escherichia coli
    • Lim CJ, Gleason FK, Fuchs JA (1986) Cloning, expression, and characterization of the Anabaena thioredoxin gene in Escherichia coli. J Bacteriol 168:1258-1264
    • (1986) J Bacteriol , vol.168 , pp. 1258-1264
    • Lim, C.J.1    Gleason, F.K.2    Fuchs, J.A.3
  • 28
    • 0346103649 scopus 로고    scopus 로고
    • Thioredoxin-linked processes in cyanobacteria are as numerous as in chloroplasts, but targets are different
    • Lindahl M, Florencio FJ (2003) Thioredoxin-linked processes in cyanobacteria are as numerous as in chloroplasts, but targets are different. Proc Natl Acad Sci USA 100:16107-16112
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 16107-16112
    • Lindahl, M.1    Florencio, F.J.2
  • 29
    • 1242271986 scopus 로고    scopus 로고
    • Systematic screening of reactive cysteine proteomes
    • Lindahl M, Florencio FJ (2004) Systematic screening of reactive cysteine proteomes. Proteomics 4:448-450
    • (2004) Proteomics , vol.4 , pp. 448-450
    • Lindahl, M.1    Florencio, F.J.2
  • 31
    • 0032735140 scopus 로고    scopus 로고
    • The Arabidopsis thaliana genome encodes at least four thioredoxins m and a new prokaryotic-like thioredoxin
    • Mestres-Ortega D, Meyer Y (1999) The Arabidopsis thaliana genome encodes at least four thioredoxins m and a new prokaryotic-like thioredoxin. Gene 240:307-316
    • (1999) Gene , vol.240 , pp. 307-316
    • Mestres-Ortega, D.1    Meyer, Y.2
  • 32
    • 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
  • 33
    • 0034130987 scopus 로고    scopus 로고
    • The photoreduction of H(2)O(2) by Synechococcus sp. PCC 7942 and UTEX 625
    • Miller AG, Hunter KJ, O'Leary SJ, Hart LJ (2000) The photoreduction of H(2)O(2) by Synechococcus sp. PCC 7942 and UTEX 625. Plant Physiol 123:625-636
    • (2000) Plant Physiol , vol.123 , pp. 625-636
    • Miller, A.G.1    Hunter, K.J.2    O'Leary, S.J.3    Hart, L.J.4
  • 34
  • 35
    • 0028003648 scopus 로고
    • Deoxyribonucleotides are maintained at normal levels in a yeast thioredoxin mutant defective in DNA synthesis
    • Muller EG (1994) Deoxyribonucleotides are maintained at normal levels in a yeast thioredoxin mutant defective in DNA synthesis. J Biol Chem 269:24466-24471
    • (1994) J Biol Chem , vol.269 , pp. 24466-24471
    • Muller, E.G.1
  • 36
    • 0024961737 scopus 로고
    • Thioredoxin is essential for photosynthetic growth. The thioredoxin m gene of Anacystis nidulans
    • Muller EG, Buchanan BB (1989) Thioredoxin is essential for photosynthetic growth. The thioredoxin m gene of Anacystis nidulans. J Biol Chem 264:4008-4014
    • (1989) J Biol Chem , vol.264 , pp. 4008-4014
    • Muller, E.G.1    Buchanan, B.B.2
  • 37
    • 0030221380 scopus 로고    scopus 로고
    • The cyanobacterial thioredoxin gene is required for both photoautotrophic and heterotrophic growth
    • Navarro F, Florencio FJ (1996) The cyanobacterial thioredoxin gene is required for both photoautotrophic and heterotrophic growth. Plant Physiol 111:1067-1075
    • (1996) Plant Physiol , vol.111 , pp. 1067-1075
    • Navarro, F.1    Florencio, F.J.2
  • 38
    • 17144472877 scopus 로고    scopus 로고
    • Electron transport controls transcription of the thioredoxin gene (trxA) in the cyanobacterium Synechocystis sp. PCC 6803
    • Navarro F, Martin-Figueroa E, Florencio FJ (2000) Electron transport controls transcription of the thioredoxin gene (trxA) in the cyanobacterium Synechocystis sp. PCC 6803. Plant Mol Biol 43:23-32
    • (2000) Plant Mol Biol , vol.43 , pp. 23-32
    • Navarro, F.1    Martin-Figueroa, E.2    Florencio, F.J.3
  • 39
    • 33645500795 scopus 로고    scopus 로고
    • Microbial ecology. How a marine bacterium adapts to multiple environments
    • Pennisi E (2006) Microbial ecology. How a marine bacterium adapts to multiple environments. Science 311:1697
    • (2006) Science , vol.311 , pp. 1697
    • Pennisi, E.1
  • 40
    • 33748980307 scopus 로고    scopus 로고
    • Selecting thioredoxins for disulphide proteomics: Target proteomes of three thioredoxins from the cyanobacterium Synechocystis sp. PCC 6803
    • Pérez-Pérez ME, Florencio FJ, Lindahl M (2006) Selecting thioredoxins for disulphide proteomics: target proteomes of three thioredoxins from the cyanobacterium Synechocystis sp. PCC 6803. Proteomics 6 (Suppl 1):S186-195
    • (2006) Proteomics , vol.6 , Issue.1 SUPPL.
    • Pérez-Pérez, M.E.1    Florencio, F.J.2    Lindahl, M.3
  • 41
    • 0037166354 scopus 로고    scopus 로고
    • Protein levels of Escherichia coli thioredoxins and glutaredoxins and their relation to null mutants, growth phase, and function
    • Potamitou A, Holmgren A, Vlamis-Gardikas A (2002) Protein levels of Escherichia coli thioredoxins and glutaredoxins and their relation to null mutants, growth phase, and function. J Biol Chem 277:18561-18567
    • (2002) J Biol Chem , vol.277 , pp. 18561-18567
    • Potamitou, A.1    Holmgren, A.2    Vlamis-Gardikas, A.3
  • 42
    • 0018409915 scopus 로고
    • Generic assignments, strain histories and properties of pure cultures of cyanobacteria
    • Rippka R, Deruelles J, Waterbury JB, Herman M, Stanier RY (1979) Generic assignments, strain histories and properties of pure cultures of cyanobacteria. J Gen Microbiol 111:1-61
    • (1979) J Gen Microbiol , vol.111 , pp. 1-61
    • Rippka, R.1    Deruelles, J.2    Waterbury, J.B.3    Herman, M.4    Stanier, R.Y.5
  • 47
    • 0023665183 scopus 로고
    • Purification and characterization of RNA polymerase from the cyanobacterium Anabaena 7120
    • Schneider GJ, Tumer NE, Richaud C, Borbely G, Haselkorn R (1987) Purification and characterization of RNA polymerase from the cyanobacterium Anabaena 7120. J Biol Chem 262:14633-14639
    • (1987) J Biol Chem , vol.262 , pp. 14633-14639
    • Schneider, G.J.1    Tumer, N.E.2    Richaud, C.3    Borbely, G.4    Haselkorn, R.5
  • 48
    • 6344235622 scopus 로고    scopus 로고
    • A novel NADPH thioredoxin reductase, localized in the chloroplast, which deficiency causes hypersensitivity to abiotic stress in Arabidopsis thaliana
    • Serrato AJ, Pérez-Ruiz JM, Spinola MC, Cejudo FJ (2004) A novel NADPH thioredoxin reductase, localized in the chloroplast, which deficiency causes hypersensitivity to abiotic stress in Arabidopsis thaliana. J Biol Chem 279:43821-43827
    • (2004) J Biol Chem , vol.279 , pp. 43821-43827
    • Serrato, A.J.1    Pérez-Ruiz, J.M.2    Spinola, M.C.3    Cejudo, F.J.4
  • 49
    • 0017263448 scopus 로고
    • The biosynthesis of multi-L-arginyl-poly(L-aspartic acid) in the filamentous cyanobacterium Anabaena cylindrica
    • Simon RD (1976) The biosynthesis of multi-L-arginyl-poly(L-aspartic acid) in the filamentous cyanobacterium Anabaena cylindrica. Biochim Biophys Acta 422:407-418
    • (1976) Biochim Biophys Acta , vol.422 , pp. 407-418
    • Simon, R.D.1
  • 50
    • 0033212766 scopus 로고    scopus 로고
    • Thiol redox state regulates expression of psbA genes in Synechococcus sp. PCC 7942
    • Sippola K, Aro EM (1999) Thiol redox state regulates expression of psbA genes in Synechococcus sp. PCC 7942. Plant Mol Biol 41:425-433
    • (1999) Plant Mol Biol , vol.41 , pp. 425-433
    • Sippola, K.1    Aro, E.M.2
  • 51
    • 0037160071 scopus 로고    scopus 로고
    • The C-terminal extension of glyceraldehyde-3-phosphate dehydrogenase subunit B acts as an autoinhibitory domain regulated by thioredoxins and nicotinamide adenine dinucleotide
    • Sparla F, Pupillo P, Trost P (2002) The C-terminal extension of glyceraldehyde-3-phosphate dehydrogenase subunit B acts as an autoinhibitory domain regulated by thioredoxins and nicotinamide adenine dinucleotide. J Biol Chem 277:44946-44952
    • (2002) J Biol Chem , vol.277 , pp. 44946-44952
    • Sparla, F.1    Pupillo, P.2    Trost, P.3
  • 52
    • 0027462109 scopus 로고
    • Purification and characterization of 5-aminolaevulinic acid dehydratase from Escherichia coli and a study of the reactive thiols at the metal-binding domain
    • Spencer P, Jordan PM (1993) Purification and characterization of 5-aminolaevulinic acid dehydratase from Escherichia coli and a study of the reactive thiols at the metal-binding domain. Biochem J 290(Pt 1):279-287
    • (1993) Biochem J , vol.290 , Issue.PART 1 , pp. 279-287
    • Spencer, P.1    Jordan, P.M.2
  • 53
    • 0032987969 scopus 로고    scopus 로고
    • In vivo role of catalase-peroxidase in Synechocystis sp. strain PCC 6803
    • Tichy M, Vermaas W (1999) In vivo role of catalase-peroxidase in Synechocystis sp. strain PCC 6803. J Bacteriol 181:1875-1882
    • (1999) J Bacteriol , vol.181 , pp. 1875-1882
    • Tichy, M.1    Vermaas, W.2
  • 54
    • 0033538442 scopus 로고    scopus 로고
    • In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family
    • Verdoucq L, Vignols F, Jacquot JP, Chartier Y, Meyer Y (1999) In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family. J Biol Chem 274:19714-19722
    • (1999) J Biol Chem , vol.274 , pp. 19714-19722
    • Verdoucq, L.1    Vignols, F.2    Jacquot, J.P.3    Chartier, Y.4    Meyer, Y.5
  • 55
    • 28044457914 scopus 로고    scopus 로고
    • A yeast two-hybrid knockout strain to explore thioredoxin-interacting proteins in vivo
    • Vignols F, Brehelin C, Surdin-Kerjan Y, Thomas D, Meyer Y. (2005) A yeast two-hybrid knockout strain to explore thioredoxin-interacting proteins in vivo. Proc Natl Acad Sci USA 102:16729-16734
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16729-16734
    • Vignols, F.1    Brehelin, C.2    Surdin-Kerjan, Y.3    Thomas, D.4    Meyer, Y.5
  • 56
    • 0030822030 scopus 로고    scopus 로고
    • Identification of the cysteine residues involved in redox modification of plant plastidic glucose-6-phosphate dehydrogenase
    • Wenderoth I, Scheibe R, von Schaewen A (1997) Identification of the cysteine residues involved in redox modification of plant plastidic glucose-6-phosphate dehydrogenase. J Biol Chem 272:26985-26990
    • (1997) J Biol Chem , vol.272 , pp. 26985-26990
    • Wenderoth, I.1    Scheibe, R.2    Von Schaewen, A.3
  • 57
    • 0028168930 scopus 로고
    • Insertion of a "chloroplast-like" regulatory segment responsible for thiol modulation into gamma-subunit of F0F1-ATPase of the cyanobacterium Synechocystis 6803 by mutagenesis of atpC
    • Werner-Grune S, Gunkel D, Schumann J, Strotmann H (1994) Insertion of a "chloroplast-like" regulatory segment responsible for thiol modulation into gamma-subunit of F0F1-ATPase of the cyanobacterium Synechocystis 6803 by mutagenesis of atpC. Mol Gen Genet 244:144-150
    • (1994) Mol Gen Genet , vol.244 , pp. 144-150
    • Werner-Grune, S.1    Gunkel, D.2    Schumann, J.3    Strotmann, H.4
  • 59
    • 0029080757 scopus 로고
    • Mixed disulfide intermediates during the reduction of disulfides by Escherichia coli thioredoxin
    • Wynn R, Cocco MJ, Richards FM (1995) Mixed disulfide intermediates during the reduction of disulfides by Escherichia coli thioredoxin. Biochemistry 34:11807-11813
    • (1995) Biochemistry , vol.34 , pp. 11807-11813
    • Wynn, R.1    Cocco, M.J.2    Richards, F.M.3
  • 62
    • 0036744350 scopus 로고    scopus 로고
    • Disulfide proteome in the analysis of protein function and structure
    • Yano H, Kuroda S, Buchanan BB (2002) Disulfide proteome in the analysis of protein function and structure. Proteomics 2:1090-1096
    • (2002) Proteomics , vol.2 , pp. 1090-1096
    • Yano, H.1    Kuroda, S.2    Buchanan, B.B.3
  • 65
    • 0037022664 scopus 로고    scopus 로고
    • Light modulation of Rubisco in Arabidopsis requires a capacity for redox regulation of the larger Rubisco activase isoform
    • Zhang N, Kallis RP, Ewy RG, Portis AR Jr (2002) Light modulation of Rubisco in Arabidopsis requires a capacity for redox regulation of the larger Rubisco activase isoform. Proc Natl Acad Sci USA 99:3330-3334
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 3330-3334
    • Zhang, N.1    Kallis, R.P.2    Ewy, R.G.3    Portis Jr., A.R.4
  • 66
    • 0033529948 scopus 로고    scopus 로고
    • Mechanism of light regulation of Rubisco: A specific role for the larger Rubisco activase isoform involving reductive activation by thioredoxin-f
    • Zhang N, Portis AR Jr (1999) Mechanism of light regulation of Rubisco: a specific role for the larger Rubisco activase isoform involving reductive activation by thioredoxin-f. Proc Natl Acad Sci USA 96:9438-9443
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9438-9443
    • Zhang, N.1    Portis Jr., A.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.