Characterization of plastidial thioredoxins from Arabidopsis belonging to the new y-type

Collin V, Lamkemeyer P, Miginiac-Maslow M, Hirasawa M, Knaff DB, Dietz K-J, Issakidis-Bourguet E (2004)
PLANT PHYSIOLOGY 136(4): 4088-4095.

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Autor*in
Collin, V; Lamkemeyer, P; Miginiac-Maslow, M; Hirasawa, M; Knaff, DB; Dietz, Karl-JosefUniBi; Issakidis-Bourguet, E
Abstract / Bemerkung
The plant plastidial thioredoxins (Trx) are involved in the light-dependent regulation of many enzymatic activities, owing to their thiol-disulfide interchange activity. Three different types of plastidial Trx have been identified and characterized so far: the m-, f-, and x-types. Recently, a new putative plastidial type, the y-type, was found. In this work the two isoforms of Trx y encoded by the nuclear genome of Arabidopsis (Arabidopsis thaliana) were characterized. The plastidial targeting of Trx y has been established by the expression of a Trx::GFP fusion protein. Then both isoforms were produced as recombinant proteins in their putative mature forms and purified to characterize them by a biochemical approach. Their ability to activate two plastidial light-regulated enzymes, NADP-malate dehydrogenase (NADP-MDH) and fructose-1,6-bisphosphatase, was tested. Both Trx y were poor activators of fructose-1,6-bisphosphatase and NADP-MDH; however, a detailed study of the activation of NADP-MDH using site-directed mutants of its regulatory cysteines suggested that Trx y was able to reduce the less negative regulatory disulfide but not the more negative regulatory disulfide. This property probably results from the fact that Trx y has a less negative redox midpoint potential (-337 mV at pH 7.9) than thioredoxins f and m. The y-type Trxs were also the best substrate for the plastidial peroxiredoxin Q. Gene expression analysis showed that Trx y2 was mainly expressed in leaves and induced by light, whereas Trx y1 was mainly expressed in nonphotosynthetic organs, especially in seeds at a stage of major accumulation of storage lipids.
Erscheinungsjahr
2004
Zeitschriftentitel
PLANT PHYSIOLOGY
Band
136
Ausgabe
4
Seite(n)
4088-4095
ISSN
0032-0889
eISSN
1532-2548
Page URI
https://pub.uni-bielefeld.de/record/1605426

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Collin V, Lamkemeyer P, Miginiac-Maslow M, et al. Characterization of plastidial thioredoxins from Arabidopsis belonging to the new y-type. PLANT PHYSIOLOGY. 2004;136(4):4088-4095.
Collin, V., Lamkemeyer, P., Miginiac-Maslow, M., Hirasawa, M., Knaff, D. B., Dietz, K. - J., & Issakidis-Bourguet, E. (2004). Characterization of plastidial thioredoxins from Arabidopsis belonging to the new y-type. PLANT PHYSIOLOGY, 136(4), 4088-4095. https://doi.org/10.1104/pp.104.052233
Collin, V, Lamkemeyer, P, Miginiac-Maslow, M, Hirasawa, M, Knaff, DB, Dietz, Karl-Josef, and Issakidis-Bourguet, E. 2004. “Characterization of plastidial thioredoxins from Arabidopsis belonging to the new y-type”. PLANT PHYSIOLOGY 136 (4): 4088-4095.
Collin, V., Lamkemeyer, P., Miginiac-Maslow, M., Hirasawa, M., Knaff, D. B., Dietz, K. - J., and Issakidis-Bourguet, E. (2004). Characterization of plastidial thioredoxins from Arabidopsis belonging to the new y-type. PLANT PHYSIOLOGY 136, 4088-4095.
Collin, V., et al., 2004. Characterization of plastidial thioredoxins from Arabidopsis belonging to the new y-type. PLANT PHYSIOLOGY, 136(4), p 4088-4095.
V. Collin, et al., “Characterization of plastidial thioredoxins from Arabidopsis belonging to the new y-type”, PLANT PHYSIOLOGY, vol. 136, 2004, pp. 4088-4095.
Collin, V., Lamkemeyer, P., Miginiac-Maslow, M., Hirasawa, M., Knaff, D.B., Dietz, K.-J., Issakidis-Bourguet, E.: Characterization of plastidial thioredoxins from Arabidopsis belonging to the new y-type. PLANT PHYSIOLOGY. 136, 4088-4095 (2004).
Collin, V, Lamkemeyer, P, Miginiac-Maslow, M, Hirasawa, M, Knaff, DB, Dietz, Karl-Josef, and Issakidis-Bourguet, E. “Characterization of plastidial thioredoxins from Arabidopsis belonging to the new y-type”. PLANT PHYSIOLOGY 136.4 (2004): 4088-4095.

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PMID: 11898430
Oxidation-reduction properties of chloroplast thioredoxins, ferredoxin:thioredoxin reductase, and thioredoxin f-regulated enzymes.
Hirasawa M, Schurmann P, Jacquot JP, Manieri W, Jacquot P, Keryer E, Hartman FC, Knaff DB., Biochemistry 38(16), 1999
PMID: 10213627
The complex regulation of ferredoxin/thioredoxin-related genes by light and the circadian clock.
Lemaire SD, Stein M, Issakidis-Bourguet E, Keryer E, Benoit V V, Pineau B, Gerard-Hirne C, Miginiac-Maslow M, Jacquot JP., Planta 209(2), 1999
PMID: 10436225
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