메뉴 건너뛰기




Volumn 188-189, Issue , 2012, Pages 82-88

Plastid thioredoxins f and m are related to the developing and salinity response of post-germinating seeds of Pisum sativum

Author keywords

Ferredoxin NADP reductase; Glucose 6 phosphate dehydrogenase; Pea; Salinity stress; Seedlings; Thioredoxin; Yeast

Indexed keywords

ISOPROTEIN; PLANT RNA; THIOREDOXIN;

EID: 84860113638     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2012.01.006     Document Type: Article
Times cited : (19)

References (37)
  • 2
    • 0036413565 scopus 로고    scopus 로고
    • The ferredoxin/thioredoxin system: from discovery to molecular structures and beyond
    • Buchanan B.B., Schurmann P., Wolosiuk R.A., Jacquot J.P. The ferredoxin/thioredoxin system: from discovery to molecular structures and beyond. Photosynth. Res. 2002, 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
  • 3
    • 65249109913 scopus 로고    scopus 로고
    • Comparative genomic study of the thioredoxin family in photosynthetic organisms with emphasis on Populus trichocarpa
    • Chibani K., Wingsle G., Jacquot J.P., Gelhaye E., Rouhier N. Comparative genomic study of the thioredoxin family in photosynthetic organisms with emphasis on Populus trichocarpa. Mol. Plant 2009, 2:308-322.
    • (2009) Mol. Plant , vol.2 , pp. 308-322
    • Chibani, K.1    Wingsle, G.2    Jacquot, J.P.3    Gelhaye, E.4    Rouhier, N.5
  • 6
    • 39749087640 scopus 로고    scopus 로고
    • Distribution of thioredoxins f and m with respect to seven light-activated enzymes and three redox-insensitive proteins in pea leaf chloroplasts
    • Anderson L.E., Fadowole D., Reyes B.A., Carol A.A. Distribution of thioredoxins f and m with respect to seven light-activated enzymes and three redox-insensitive proteins in pea leaf chloroplasts. Plant Sci. 2008, 174:432-445.
    • (2008) Plant Sci. , vol.174 , pp. 432-445
    • Anderson, L.E.1    Fadowole, D.2    Reyes, B.A.3    Carol, A.A.4
  • 7
    • 0033166052 scopus 로고    scopus 로고
    • Chloroplast thioredoxin mutants without active-site cysteines facilitate the reduction of the regulatory disulphide bridge on the gamma-subunit of chloroplast ATP synthase
    • Stumpp M.T., Motohashi K., Hisabori T. Chloroplast thioredoxin mutants without active-site cysteines facilitate the reduction of the regulatory disulphide bridge on the gamma-subunit of chloroplast ATP synthase. Biochem. J. 1999, 341(Pt 1):157-163.
    • (1999) Biochem. J. , vol.341 , Issue.PART 1 , pp. 157-163
    • Stumpp, M.T.1    Motohashi, K.2    Hisabori, T.3
  • 10
    • 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 A.J., Pérez-Ruiz J.M., Spinola M.C., Cejudo F.J. A novel NADPH thioredoxin reductase, localized in the chloroplast, which deficiency causes hypersensitivity to abiotic stress in Arabidopsis thaliana. J. Biol. Chem. 2004, 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
  • 11
    • 0026829153 scopus 로고
    • Isolation, characterization and nucleotide sequence of a full-length pea cDNA encoding thioredoxin-f
    • Lepiniec L., Hodges M., Gadal P., Cretin C. Isolation, characterization and nucleotide sequence of a full-length pea cDNA encoding thioredoxin-f. Plant Mol. Biol. 1992, 18:1023-1025.
    • (1992) Plant Mol. Biol. , vol.18 , pp. 1023-1025
    • Lepiniec, L.1    Hodges, M.2    Gadal, P.3    Cretin, C.4
  • 14
    • 77952237237 scopus 로고    scopus 로고
    • The chloroplastic thiol reducing systems: dual functions in the regulation of carbohydrate metabolism and regeneration of antioxidant enzymes, emphasis on the poplar redoxin equipment
    • Chibani K., Couturier J., Selles B., Jacquot J.P., Rouhier N. The chloroplastic thiol reducing systems: dual functions in the regulation of carbohydrate metabolism and regeneration of antioxidant enzymes, emphasis on the poplar redoxin equipment. Photosynth. Res. 2010, 104:75-99.
    • (2010) Photosynth. Res. , vol.104 , pp. 75-99
    • Chibani, K.1    Couturier, J.2    Selles, B.3    Jacquot, J.P.4    Rouhier, N.5
  • 15
    • 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
  • 18
    • 0037795745 scopus 로고    scopus 로고
    • The oxidative pentose phosphate pathway: structure and organisation
    • Kruger N.J., von Schaewen A. The oxidative pentose phosphate pathway: structure and organisation. Curr. Opin. Plant Biol. 2003, 6:236-246.
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 236-246
    • Kruger, N.J.1    von Schaewen, A.2
  • 19
    • 36248936703 scopus 로고    scopus 로고
    • Localization in roots and flowers of pea chloroplastic thioredoxin f and thioredoxin m proteins reveals new roles in nonphotosynthetic organs
    • Barajas-López J.D., Serrato A.J., Olmedilla A., Chueca A., Sahrawy M. Localization in roots and flowers of pea chloroplastic thioredoxin f and thioredoxin m proteins reveals new roles in nonphotosynthetic organs. Plant Physiol. 2007, 145:946-960.
    • (2007) Plant Physiol. , vol.145 , pp. 946-960
    • Barajas-López, J.D.1    Serrato, A.J.2    Olmedilla, A.3    Chueca, A.4    Sahrawy, M.5
  • 21
    • 0038038334 scopus 로고    scopus 로고
    • Identification and differential expression of two thioredoxin h isoforms in germinating seeds from pea
    • Montrichard F., Renard M., Alkhalfioui F., Duval F.D., Macherel D. Identification and differential expression of two thioredoxin h isoforms in germinating seeds from pea. Plant Physiol. 2003, 132:1707-1715.
    • (2003) Plant Physiol. , vol.132 , pp. 1707-1715
    • Montrichard, F.1    Renard, M.2    Alkhalfioui, F.3    Duval, F.D.4    Macherel, D.5
  • 23
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bio assays with tobacco tissue cultures
    • Murashige Y., Skoog F. A revised medium for rapid growth and bio assays with tobacco tissue cultures. Physiol. Plant. 1962, 15:473-497.
    • (1962) Physiol. Plant. , vol.15 , pp. 473-497
    • Murashige, Y.1    Skoog, F.2
  • 24
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-ΔΔC(T)) method
    • Livak K.J., Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-ΔΔC(T)) method. Methods 2001, 25:402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 25
    • 0342444416 scopus 로고
    • GUS fusions: beta-glucuronidase as a sensitive and versatile gene fusion marker in higher plants
    • Jefferson R.A., Kavanagh T.A., Bevan M.W. GUS fusions: beta-glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J. 1987, 6:3901-3907.
    • (1987) EMBO J. , vol.6 , pp. 3901-3907
    • Jefferson, R.A.1    Kavanagh, T.A.2    Bevan, M.W.3
  • 26
    • 0025740886 scopus 로고
    • Thioredoxin deficiency in yeast prolongs S phase and shortens the G1 interval of the cell cycle
    • Muller E.G. Thioredoxin deficiency in yeast prolongs S phase and shortens the G1 interval of the cell cycle. J. Biol. Chem. 1991, 266:9194-9202.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9194-9202
    • Muller, E.G.1
  • 27
    • 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., Miginiac-Maslow M. Heterologous complementation of yeast reveals a new putative function for chloroplast m-type thioredoxin. Plant J. 2001, 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
  • 28
    • 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., Meyer Y. In vivo functional discrimination between plant thioredoxins by heterologous expression in the yeast Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 1998, 95:3312-3317.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 3312-3317
    • Mouaheb, N.1    Thomas, D.2    Verdoucq, L.3    Monfort, P.4    Meyer, Y.5
  • 29
    • 0026864596 scopus 로고
    • Complementation of Saccharomyces cerevisiae auxotrophic mutants by Arabidopsis thaliana cDNAs
    • Minet M., Dufour M.E., Lacroute F. Complementation of Saccharomyces cerevisiae auxotrophic mutants by Arabidopsis thaliana cDNAs. Plant J. 1992, 2:417-422.
    • (1992) Plant J. , vol.2 , pp. 417-422
    • Minet, M.1    Dufour, M.E.2    Lacroute, F.3
  • 31
    • 0034623172 scopus 로고    scopus 로고
    • Specific expression of glucose-6-phosphate dehydrogenase (G6PDH) gene by salt stress in wheat (Triticum aestivum L.)
    • Nemoto Y., Sasakuma T. Specific expression of glucose-6-phosphate dehydrogenase (G6PDH) gene by salt stress in wheat (Triticum aestivum L.). Plant Sci. 2000, 158:53-60.
    • (2000) Plant Sci. , vol.158 , pp. 53-60
    • Nemoto, Y.1    Sasakuma, T.2
  • 33
    • 0034056617 scopus 로고    scopus 로고
    • Dof1 and Dof2 transcription factors are associated with expression of multiple genes involved in carbon metabolism in maize
    • Yanagisawa S. Dof1 and Dof2 transcription factors are associated with expression of multiple genes involved in carbon metabolism in maize. Plant J. 2000, 21:281-288.
    • (2000) Plant J. , vol.21 , pp. 281-288
    • Yanagisawa, S.1
  • 34
    • 0642340497 scopus 로고    scopus 로고
    • Genome-wide comparative phylogenetic analysis of the rice and Arabidopsis Dof gene families
    • Lijavetzky D., Carbonero P., Vicente-Carbajosa J. Genome-wide comparative phylogenetic analysis of the rice and Arabidopsis Dof gene families. BMC Evol. Biol. 2003, 3:17.
    • (2003) BMC Evol. Biol. , vol.3 , pp. 17
    • Lijavetzky, D.1    Carbonero, P.2    Vicente-Carbajosa, J.3
  • 35
    • 77953313350 scopus 로고    scopus 로고
    • Extracellular production of reactive oxygen species during seed germination and early seedling growth in Pisum sativum
    • Kranner I., Roach T., Beckett R.P., Whitaker C., Minibayeva F.V. Extracellular production of reactive oxygen species during seed germination and early seedling growth in Pisum sativum. J. Plant Physiol. 2010, 167:805-811.
    • (2010) J. Plant Physiol. , vol.167 , pp. 805-811
    • Kranner, I.1    Roach, T.2    Beckett, R.P.3    Whitaker, C.4    Minibayeva, F.V.5
  • 37
    • 0034928212 scopus 로고    scopus 로고
    • Characterization of two thioredoxins h with predominant localization in the nucleus of aleurone and scutellum cells of germinating wheat seeds
    • Serrato A.J., Crespo J.L., Florencio F.J., Cejudo F.J. Characterization of two thioredoxins h with predominant localization in the nucleus of aleurone and scutellum cells of germinating wheat seeds. Plant Mol. Biol. 2001, 46:361-371.
    • (2001) Plant Mol. Biol. , vol.46 , pp. 361-371
    • Serrato, A.J.1    Crespo, J.L.2    Florencio, F.J.3    Cejudo, F.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.