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Volumn 2, Issue 2, 2009, Pages 270-283

Photosynthetic regulation of the cyanobacterium synechocystis sp. PCC 6803 thioredoxin system and functional analysis of TrxB (Trx x) and TrxQ (Trx y) thioredoxins

Author keywords

Cyanobacteria; Oxidative stress; Photosynthetic electron transport; Synechocystis; Thioredoxin

Indexed keywords

CYANOBACTERIA; SYNECHOCYSTIS; SYNECHOCYSTIS SP.; SYNECHOCYSTIS SP. PCC 6803;

EID: 65249101414     PISSN: 16742052     EISSN: 17529867     Source Type: Journal    
DOI: 10.1093/mp/ssn070     Document Type: Article
Times cited : (43)

References (60)
  • 2
    • 20044367629 scopus 로고    scopus 로고
    • Redox regulation: A broadening horizon
    • Buchanan, B.B., and 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
  • 4
    • 0037930284 scopus 로고    scopus 로고
    • The Arabidopsis plastidial thioredoxins: New functions and new insights into specificity
    • Collin, V., et al. (2003). The Arabidopsis plastidial thioredoxins: new functions and new insights into specificity. J. Biol. Chem. 278, 23747-23752.
    • (2003) J. Biol. Chem , vol.278 , pp. 23747-23752
    • Collin, V.1
  • 5
    • 16644395716 scopus 로고    scopus 로고
    • Characterization of plastidial thioredoxins from Arabidopsis belonging to the new y-type
    • Collin, V., et al. (2004). Characterization of plastidial thioredoxins from Arabidopsis belonging to the new y-type. Plant Physiol. 136, 4088-4095.
    • (2004) Plant Physiol , vol.136 , pp. 4088-4095
    • Collin, V.1
  • 6
    • 0023754017 scopus 로고
    • A versatile class of positive-selection vectors based on the nonviability of palindrome-containing plas-mids that allows cloning into long polylinkers
    • Elhai, J., and Wolk, C.P. (1988). A versatile class of positive-selection vectors based on the nonviability of palindrome-containing plas-mids that allows cloning into long polylinkers. Gene. 68, 119-138.
    • (1988) Gene , vol.68 , pp. 119-138
    • Elhai, J.1    Wolk, C.P.2
  • 8
    • 0031459965 scopus 로고    scopus 로고
    • Nitrogen availability and electron transport control the expression of glnB gene (encoding Pll protein) in the cyanobacterium Synechocystis sp. PCC 6803
    • Garcia-Dominguez, M., and Florencio, F.J. (1997). Nitrogen availability and electron transport control the expression of glnB gene (encoding Pll protein) in the cyanobacterium Synechocystis sp. PCC 6803. Plant Mol. Biol. 35, 723-734.
    • (1997) Plant Mol. Biol , vol.35 , pp. 723-734
    • Garcia-Dominguez, M.1    Florencio, F.J.2
  • 11
    • 0036286617 scopus 로고    scopus 로고
    • Genome-wide dynamic transcriptional profiling of the light-to-dark transition in Synechocystis sp. strain PCC 6803
    • Gill, R.T., Katsoulakis, E., Schmitt, W., Taroncher-Oldenburg, G., Misra, J., and Stephanopoulos, G. (2002). Genome-wide dynamic transcriptional profiling of the light-to-dark transition in Synechocystis sp. strain PCC 6803. J. Bacteriol. 184, 3671-3681.
    • (2002) J. Bacteriol , vol.184 , pp. 3671-3681
    • Gill, R.T.1    Katsoulakis, E.2    Schmitt, W.3    Taroncher-Oldenburg, G.4    Misra, J.5    Stephanopoulos, G.6
  • 12
    • 0026645607 scopus 로고
    • Activities of two dissimilar thioredoxins from the cyanobacterium Anabaena sp. strain PCC 7120
    • Gleason, F.K. (1992). Activities of two dissimilar thioredoxins from the cyanobacterium Anabaena sp. strain PCC 7120. J. Bacteriol. 174, 2592-2598.
    • (1992) J. Bacteriol , vol.174 , pp. 2592-2598
    • Gleason, F.K.1
  • 13
    • 0024147201 scopus 로고
    • Thioredoxin and related proteins in procaryotes
    • Gleason, F.K., and Holmgren, A. (1988). Thioredoxin and related proteins in procaryotes. FEMS Microbiol. Rev. 4, 271-297.
    • (1988) FEMS Microbiol. Rev , vol.4 , pp. 271-297
    • Gleason, F.K.1    Holmgren, A.2
  • 14
    • 0035037364 scopus 로고    scopus 로고
    • DNA microarray analysis of cyanobacterial gene expression during acclimation to high light
    • Hihara, Y., Kamei, A., Kanehisa, M., Kaplan, A., and Ikeuchi, M. (2001). DNA microarray analysis of cyanobacterial gene expression during acclimation to high light. Plant Cell. 13, 793-806.
    • (2001) Plant Cell , vol.13 , pp. 793-806
    • Hihara, Y.1    Kamei, A.2    Kanehisa, M.3    Kaplan, A.4    Ikeuchi, M.5
  • 15
    • 0037369852 scopus 로고    scopus 로고
    • DNA microarray analysis of redox-responsive genes in the genome of the cyanobacterium Synechocystis sp. strain PCC 6803
    • Hihara, Y, Sonoike, K., Kanehisa, M., and Ikeuchi, M. (2003). DNA microarray analysis of redox-responsive genes in the genome of the cyanobacterium Synechocystis sp. strain PCC 6803. J. Bacteriol. 185, 1719-1725.
    • (2003) J. Bacteriol , vol.185 , pp. 1719-1725
    • Hihara, Y.1    Sonoike, K.2    Kanehisa, M.3    Ikeuchi, M.4
  • 17
    • 0034534165 scopus 로고    scopus 로고
    • Antioxidant function of thioredoxin and glutaredoxin systems
    • Holmgren, A. (2000). Antioxidant function of thioredoxin and glutaredoxin systems. Antioxid. Redox. Signal. 2, 811-820.
    • (2000) Antioxid. Redox. Signal , vol.2 , pp. 811-820
    • Holmgren, A.1
  • 18
    • 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., et al. (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
  • 19
    • 0036947251 scopus 로고    scopus 로고
    • Global gene expression profiles of the cyanobacterium Synechocystis sp. strain PCC 6803 in response to irradiation with UV-B and white light
    • Huang, L., McCluskey, M.P., Ni, H., and LaRossa, R.A. (2002). Global gene expression profiles of the cyanobacterium Synechocystis sp. strain PCC 6803 in response to irradiation with UV-B and white light. J. Bacteriol. 184, 6845-6858.
    • (2002) J. Bacteriol , vol.184 , pp. 6845-6858
    • Huang, L.1    McCluskey, M.P.2    Ni, H.3    LaRossa, R.A.4
  • 20
    • 0035142197 scopus 로고    scopus 로고
    • Heterologous complementation of yeast reveals a new putative function for chloroplast m-type thioredoxin
    • Issakidis-Bourguet, E., Mouaheb, N., Meyer, Y., and Miginiac-Maslow, M. (2001). Heterologous complementation of yeast reveals a new putative function for chloroplast m-type thioredoxin. Plant J. 25, 127-135.
    • (2001) Plant J , vol.25 , pp. 127-135
    • Issakidis-Bourguet, E.1    Mouaheb, N.2    Meyer, Y.3    Miginiac-Maslow, M.4
  • 21
    • 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, H.H., 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
  • 22
    • 33846068839 scopus 로고    scopus 로고
    • Histidine kinases play important roles in the perception and signal transduction of hydrogen peroxide in the cyanobacterium, Synechocystis sp. PCC 6803
    • Kanesaki, Y, et al. (2007). Histidine kinases play important roles in the perception and signal transduction of hydrogen peroxide in the cyanobacterium, Synechocystis sp. PCC 6803. Plant J. 49, 313-324.
    • (2007) Plant J , vol.49 , pp. 313-324
    • Kanesaki, Y.1
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0032840224 scopus 로고    scopus 로고
    • Heavy-metal regulation of thioredoxin gene expression in chlamydomonas reinhardtii
    • Lemaire, S., et al. (1999). Heavy-metal regulation of thioredoxin gene expression in chlamydomonas reinhardtii. Plant Physiol. 120, 773-778.
    • (1999) Plant Physiol , vol.120 , pp. 773-778
    • Lemaire, S.1
  • 25
    • 11144323768 scopus 로고    scopus 로고
    • The thioredoxin superfamily in Chlamydomonas reinhardtii
    • Lemaire, S.D., and Miginiac-Maslow, M. (2004). The thioredoxin superfamily in Chlamydomonas reinhardtii. Photosynth. Res. 82, 203-220.
    • (2004) Photosynth. Res , vol.82 , pp. 203-220
    • Lemaire, S.D.1    Miginiac-Maslow, M.2
  • 26
    • 0038393110 scopus 로고    scopus 로고
    • Characterization of thioredoxin y, a new type of thioredoxin identified in the genome of Chlamydomonas reinhardtii
    • Lemaire, S.D., Collin, V., Keryer, E., Quesada, A., and 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
  • 29
    • 0036125713 scopus 로고    scopus 로고
    • Plant thioredoxin gene expression: Control by light, circadian clock, and heavy metals
    • Lemaire, S.D., Miginiac-Maslow, M., and Jacquot, J.P. (2002). Plant thioredoxin gene expression: control by light, circadian clock, and heavy metals. Methods Enzymol. 347, 412-421.
    • (2002) Methods Enzymol , vol.347 , pp. 412-421
    • Lemaire, S.D.1    Miginiac-Maslow, M.2    Jacquot, J.P.3
  • 30
    • 2442682940 scopus 로고    scopus 로고
    • Differential gene expression in response to hydrogen peroxide and the putative PerR regulon of Synechocystis sp. strain PCC 6803
    • Li, H., Singh, A.K., Mclntyre, L.M., and Sherman, L.A. (2004). Differential gene expression in response to hydrogen peroxide and the putative PerR regulon of Synechocystis sp. strain PCC 6803. J. Bacteriol. 186, 3331-3345.
    • (2004) J. Bacteriol , vol.186 , pp. 3331-3345
    • Li, H.1    Singh, A.K.2    Mclntyre, L.M.3    Sherman, L.A.4
  • 31
    • 0346103649 scopus 로고    scopus 로고
    • Thioredoxin-linked processes in cyanobacteria are as numerous as in chloroplasts, but targets are different
    • Lindahl, M., and Florencio, F.J. (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
  • 32
    • 0036194664 scopus 로고    scopus 로고
    • A two-component signal transduction system involved in nickel sensing in the cyanobacterium Synechocystis sp. PCC 6803
    • Lopez-Maury, L., Garcia-Dominguez, M., Florencio, F.J., and Reyes, J.C. (2002). A two-component signal transduction system involved in nickel sensing in the cyanobacterium Synechocystis sp. PCC 6803. Mol. Microbiol. 43, 247-256.
    • (2002) Mol. Microbiol , vol.43 , pp. 247-256
    • Lopez-Maury, L.1    Garcia-Dominguez, M.2    Florencio, F.J.3    Reyes, J.C.4
  • 34
    • 36048943681 scopus 로고    scopus 로고
    • Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin
    • Mata-Cabana, A., Florencio, F.J., and Lindahl, M. (2007). Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin. Proteomics. 7, 3953-3963.
    • (2007) Proteomics , vol.7 , pp. 3953-3963
    • Mata-Cabana, A.1    Florencio, F.J.2    Lindahl, M.3
  • 35
    • 29944441650 scopus 로고    scopus 로고
    • Thioredoxins in Arabidopsis and other plants
    • Meyer, Y., Reichheld, J.P., and 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
  • 37
    • 0024869570 scopus 로고
    • Influence of light on accumulation of photosynthesis-specific transcripts in the cyanobacterium Synechocystis 6803
    • Mohamed, A., and Jansson, C. (1989). Influence of light on accumulation of photosynthesis-specific transcripts in the cyanobacterium Synechocystis 6803. Plant Mol. Biol. 13, 693-700.
    • (1989) Plant Mol. Biol , vol.13 , pp. 693-700
    • Mohamed, A.1    Jansson, C.2
  • 38
    • 0026161992 scopus 로고
    • Photosynthetic electron transport controls degradation but not production of psbA transcripts in the cyanobacterium Synechocystis 6803
    • Mohamed, A., and Jansson, C. (1991). Photosynthetic electron transport controls degradation but not production of psbA transcripts in the cyanobacterium Synechocystis 6803. Plant Mol. Biol. 16, 891-897.
    • (1991) Plant Mol. Biol , vol.16 , pp. 891-897
    • Mohamed, A.1    Jansson, C.2
  • 39
    • 0027324796 scopus 로고
    • Differential expression of the psbA genes in the cyanobacterium Synechocystis 6803
    • Mohamed, A., Eriksson, J., Osiewacz, H.D., and Jansson, C. (1993). Differential expression of the psbA genes in the cyanobacterium Synechocystis 6803. Mol. Gen. Genet. 238, 161-168.
    • (1993) Mol. Gen. Genet , vol.238 , pp. 161-168
    • Mohamed, A.1    Eriksson, J.2    Osiewacz, H.D.3    Jansson, C.4
  • 40
    • 0035949574 scopus 로고    scopus 로고
    • Comprehensive survey of proteins targeted by chloroplast thioredoxin
    • Motohashi, K., Kondoh, A., Stumpp, M.T., and Hisabori, T. (2001). Comprehensive survey of proteins targeted by chloroplast thioredoxin. Proc. Natl Acad. Sci. USA. 98, 11224-11229.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 11224-11229
    • Motohashi, K.1    Kondoh, A.2    Stumpp, M.T.3    Hisabori, T.4
  • 41
    • 0032539799 scopus 로고    scopus 로고
    • In vivo functional discrimination between plant thioredoxins by heterologous expression in the yeast Saccharomyces cerevisiae
    • Mouaheb, N., Thomas, D., Verdoucq, L., Monfort, P., and Meyer, Y. (1998). In vivo functional discrimination between plant thioredoxins by heterologous expression in the yeast Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA. 95, 3312-3317.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 3312-3317
    • Mouaheb, N.1    Thomas, D.2    Verdoucq, L.3    Monfort, P.4    Meyer, Y.5
  • 42
    • 0029948308 scopus 로고    scopus 로고
    • A glutathione reductase mutant of yeast accumulates high levels of oxidized glutathione and requires thioredoxin for growth
    • Muller, E.G. (1996). A glutathione reductase mutant of yeast accumulates high levels of oxidized glutathione and requires thioredoxin for growth. Mol. Biol. Cell. 7, 1805-1813.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1805-1813
    • Muller, E.G.1
  • 43
    • 0024961737 scopus 로고
    • Thioredoxin is essential for photosynthetic growth. The thioredoxin m gene of Anacystis nidulans
    • Muller, E.G., and Buchanan, B.B. (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
  • 44
    • 0030221380 scopus 로고    scopus 로고
    • The cyanobacterial thioredoxin gene is required for both photoautotrophic and heterotrophic growth
    • Navarro, F., and Florencio, F.J. (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
  • 45
    • 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., and Florencio, F.J. (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
  • 46
    • 33748980307 scopus 로고    scopus 로고
    • Selecting thioredoxins for disulphide proteomics: Target proteomes of three thioredoxins from the cyanobacterium Synechocystis sp. PCC 6803
    • Perez-Perez, M.E., Florencio, F.J., and 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-S195.
    • (2006) Proteomics , vol.6 , Issue.SUPPL. 1
    • Perez-Perez, M.E.1    Florencio, F.J.2    Lindahl, M.3
  • 47
    • 0021592032 scopus 로고
    • In vitro insertional mutagenesis with a selectable DNA fragment
    • Prentki, P., and Krisch, H.M. (1984). In vitro insertional mutagenesis with a selectable DNA fragment. Gene. 29, 303-313.
    • (1984) Gene , vol.29 , pp. 303-313
    • Prentki, P.1    Krisch, H.M.2
  • 48
    • 30044436319 scopus 로고    scopus 로고
    • The thioredoxin system protects ribosomes against stress-induced aggregation
    • Rand, J.D., and Grant, CM. (2006). The thioredoxin system protects ribosomes against stress-induced aggregation. Mol. Biol. Cell. 17, 387-401.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 387-401
    • Rand, J.D.1    Grant, C.M.2
  • 49
    • 0029240530 scopus 로고
    • Electron transport controls transcription of the glutamine synthetase gene (glnA) from the cyanobacterium Synechocystis sp. PCC 6803
    • Reyes, J.C., and Florencio, F.J. (1995). Electron transport controls transcription of the glutamine synthetase gene (glnA) from the cyanobacterium Synechocystis sp. PCC 6803. Plant Mol. Biol. 27, 789-799.
    • (1995) Plant Mol. Biol , vol.27 , pp. 789-799
    • Reyes, J.C.1    Florencio, F.J.2
  • 50
    • 0018409915 scopus 로고
    • Generic assignement, strain histories and properties of purecultures of cyanobacteria
    • Rippka, R., Deruelles, J., Waterbury, J.B., Herdman, M., and Stanier, R.Y. (1979). Generic assignement, strain histories and properties of purecultures 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    Herdman, M.4    Stanier, R.Y.5
  • 51
    • 12144287638 scopus 로고    scopus 로고
    • Poplar peroxiredoxin Q: A thioredoxin-linked chloroplast antioxidant functional in pathogen defense
    • Rouhier, N., et al. (2004). Poplar peroxiredoxin Q: a thioredoxin-linked chloroplast antioxidant functional in pathogen defense. Plant Physiol. 134, 1027-1038.
    • (2004) Plant Physiol , vol.134 , pp. 1027-1038
    • Rouhier, N.1
  • 52
    • 42949151399 scopus 로고    scopus 로고
    • The ferredoxin/thiore- doxin system of oxygenic photosynthesis
    • Schurmann, P., and Buchanan, B.B. (2008). The ferredoxin/thiore- doxin system of oxygenic photosynthesis. Antioxid. Redox. Signal. 10, 1235-1274.
    • (2008) Antioxid. Redox. Signal , vol.10 , pp. 1235-1274
    • Schurmann, P.1    Buchanan, B.B.2
  • 53
    • 45249107767 scopus 로고    scopus 로고
    • AtCXXS: Atypical members of the Arabidopsis thaliana thioredoxin h family with a remarkably high disulfide isomerase activity
    • Serrato, A.J., Guilleminot, J., Meyer, Y, and Vignols, F. (2008). AtCXXS: atypical members of the Arabidopsis thaliana thioredoxin h family with a remarkably high disulfide isomerase activity. Physiol. Plant. 133, 611-622.
    • (2008) Physiol. Plant , vol.133 , pp. 611-622
    • Serrato, A.J.1    Guilleminot, J.2    Meyer, Y.3    Vignols, F.4
  • 54
    • 0026261666 scopus 로고
    • Expression of photosynthesis genes in the cyanobacterium Synechocystis sp. PCC 6803: PsaA-psaB and psbA transcripts accumulate in dark-grown cells
    • Smart, LB., and Mcintosh, L. (1991). Expression of photosynthesis genes in the cyanobacterium Synechocystis sp. PCC 6803: psaA-psaB and psbA transcripts accumulate in dark-grown cells. Plant Mol. Biol. 17, 959-971.
    • (1991) Plant Mol. Biol , vol.17 , pp. 959-971
    • Smart, L.B.1    Mcintosh, L.2
  • 55
    • 0032473824 scopus 로고    scopus 로고
    • Acquisition of a new type of fructose-1,6-bisphosphatase with resistance to hydrogen peroxide in cyanobacteria: Molecular characterization of the enzyme from Synechocystis PCC 6803
    • Tamoi, M., Murakami, A., Takeda, T., and Shigeoka, S. (1998). Acquisition of a new type of fructose-1,6-bisphosphatase with resistance to hydrogen peroxide in cyanobacteria: molecular characterization of the enzyme from Synechocystis PCC 6803. Biochim. Biophys. Acta. 1383, 232-244.
    • (1998) Biochim. Biophys. Acta , vol.1383 , pp. 232-244
    • Tamoi, M.1    Murakami, A.2    Takeda, T.3    Shigeoka, S.4
  • 56
    • 0036435926 scopus 로고    scopus 로고
    • Thioredoxins are required for protection against a reductive stress in the yeast Saccharomyces cerevisiae
    • Trotter, E.W., and Grant, CM. (2002). Thioredoxins are required for protection against a reductive stress in the yeast Saccharomyces cerevisiae. Mol. Microbiol. 46, 869-878.
    • (2002) Mol. Microbiol , vol.46 , pp. 869-878
    • Trotter, E.W.1    Grant, C.M.2
  • 57
    • 28044457914 scopus 로고    scopus 로고
    • A yeast two-hybrid knockout strain to explore thiore-doxin-interacting proteins in vivo
    • Vignols, F., Brehelin, C., Surdin-Kerjan, Y., Thomas, D., and Meyer, Y. (2005). A yeast two-hybrid knockout strain to explore thiore-doxin-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
  • 58
    • 0027053219 scopus 로고
    • Analysis of the gene encoding the RNA subunit of ribonuclease P from cyanobacteria
    • Vioque, A. (1992). Analysis of the gene encoding the RNA subunit of ribonuclease P from cyanobacteria. Nucleic Acids Res. 20, 6331-6337.
    • (1992) Nucleic Acids Res , vol.20 , pp. 6331-6337
    • Vioque, A.1
  • 59
    • 0036125983 scopus 로고    scopus 로고
    • Identification of thioredoxin-linked proteins by fluorescence labeling combined with isoelectric focusing/sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Wong, J.H., Yano, H., Lee, Y.M., Cho, M.J., and Buchanan, B.B. (2002). Identification of thioredoxin-linked proteins by fluorescence labeling combined with isoelectric focusing/sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Methods Enzymol. 347, 339-349.
    • (2002) Methods Enzymol , vol.347 , pp. 339-349
    • Wong, J.H.1    Yano, H.2    Lee, Y.M.3    Cho, M.J.4    Buchanan, B.B.5
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.