AtCXXS: atypical members of the Arabidopsis thaliana thioredoxin h family with a remarkably high disulfide isomerase activity

Authors: Serrato, Antonio Jesús; Guilleminot, Jocelyne; Meyer, Yves; Vignols, Florence

Source: Physiologia Plantarum, Volume 133, Number 3, July 2008 , pp. 611-622(12)

Publisher: Wiley-Blackwell

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Abstract:

The Arabidopsis thaliana thioredoxin subgroup h III is composed of four members and includes the two monocysteinic (CXXS) thioredoxins encoded by the genome. We show that AtCXXS1 is the ortholog of monocysteinic thioredoxins present in all higher plants. In contrast, unicellular algae and the moss Physcomitrella patens do not encode monocysteinic thioredoxin. AtCXXS2, the second monocysteinic thioredoxin of Arabidopsis has no ortholog in any other higher plants. It probably appeared recently by duplications of a dicysteinic thioredoxin of the same subgroup h III. Both monocysteinic thioredoxins show a low disulfide reductase activity in vitro but are very efficient as disulfide isomerases in RNAse refolding tests. The possible interactions of these proteins with the glutathione glutaredoxin pathway are discussed on the basis of recent papers.

Document Type: Research article

DOI: http://dx.doi.org/10.1111/j.1399-3054.2008.01093.x

Affiliations: 1: Laboratoire Génome et Développement des Plantes, UMR CNRS-IRD-UPVD 5096, Université de Perpignan, Perpignan, Cedex, France

Publication date: 2008-07-01

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