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.

Journal Article | Published | English

No fulltext has been uploaded

Author
; ; ; ; ; ;
Abstract
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.
Publishing Year
ISSN
eISSN
PUB-ID

Cite this

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.
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.
This data publication is cited in the following publications:
This publication cites the following data publications:

62 Citations in Europe PMC

Data provided by Europe PubMed Central.

Thioredoxin Selectivity for Thiol-based Redox Regulation of Target Proteins in Chloroplasts.
Yoshida K, Hara S, Hisabori T., J. Biol. Chem. 290(23), 2015
PMID: 25878252
A comprehensive study of thiol reduction gene expression under stress conditions in Arabidopsis thaliana.
Belin C, Bashandy T, Cela J, Delorme-Hinoux V, Riondet C, Reichheld JP., Plant Cell Environ. 38(2), 2015
PMID: 24428628
Overexpression of plastidial thioredoxins f and m differentially alters photosynthetic activity and response to oxidative stress in tobacco plants.
Rey P, Sanz-Barrio R, Innocenti G, Ksas B, Courteille A, Rumeau D, Issakidis-Bourguet E, Farran I., Front Plant Sci 4(), 2013
PMID: 24137166
Quantitative proteomics of tomato defense against Pseudomonas syringae infection.
Parker J, Koh J, Yoo MJ, Zhu N, Feole M, Yi S, Chen S., Proteomics 13(12-13), 2013
PMID: 23533086
Redox regulation of carbonic anhydrases via thioredoxin in chloroplast of the marine diatom Phaeodactylum tricornutum.
Kikutani S, Tanaka R, Yamazaki Y, Hara S, Hisabori T, Kroth PG, Matsuda Y., J. Biol. Chem. 287(24), 2012
PMID: 22535967
The conformational stability and biophysical properties of the eukaryotic thioredoxins of Pisum sativum are not family-conserved.
Aguado-Llera D, Martinez-Gomez AI, Prieto J, Marenchino M, Traverso JA, Gomez J, Chueca A, Neira JL., PLoS ONE 6(2), 2011
PMID: 21364950
Thioredoxin h System and Wheat Seed Quality.
Zahid Abderrakib, Afoulous Samia, Cazalis Roland., 2008
PMID: IND44130488

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 15531707
PubMed | Europe PMC

Search this title in

Google Scholar