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JXB Advance Access originally published online on August 27, 2004
Journal of Experimental Botany 2004 55(406):2191-2199; doi:10.1093/jxb/erh238
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Journal of Experimental Botany, Vol. 55, No. 406, © Society for Experimental Biology 2004; all rights reserved

RESEARCH PAPER

Cloning and characterization of a 2-Cys peroxiredoxin from Pisum sativum

Laura Bernier-Villamor1, Eusebio Navarro2, Francisca Sevilla2 and Juan-José Lázaro1,*

1Departamento de Bioquímica, Biología Molecular y Celular de Plantas, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Científicas, E-18008, Granada, Spain
2Departamento de Nutrición y Fisiología Vegetal, Centro de Edafología y Biología Aplicada del Segura, Consejo Superior de Investigaciones Científicas, E-30080, Murcia, Spain

* To whom correspondence should be addressed. Fax: +34 958 129600. E-mail: jjlazaro{at}eez.csic.es

A cDNA sequence coding for a pea (Pisum sativum L.) 2-Cys peroxiredoxin (2-Cys Prx) has been cloned. The deduced amino acid sequence showed a high sequence homology to the 2-Cys Prx enzymes of Phaseolus vulgaris (86%), Arabidopsis thaliana (75%), and Spinacia oleracea (75%), and contained a chloroplast target sequence at its N-terminus. The mature enzyme, without the transit peptide, has a molecular mass of 22 kDa as well as two cysteine residues (Cys-53 and Cys-175) which are well conserved among proteins of this group. The protein was expressed in a heterologous system using the expression vector pET3d, and was purified to homogeneity by three sequential chromatographic steps. The enzyme exhibits peroxidase activity on hydrogen peroxide (H2O2) and t-butyl hydroperoxide (TBHP) with DTT as reducing agent. Although both pea Trxs f and m reduce oxidized 2-Cys Prx, Trx m is more efficient. The precise conditions for oligomerization of 2-Cys Prx through extensive gel filtration studies are also reported. The transition dimer–decamer produced in vitro between pH 7.5 and 8.0 and the influence of DTT suggest that a great change in the enzyme quaternary structure of 2-Cys Prx may take place in the chloroplast during the dark–light transition. In addition, the cyclophilin-dependent reduction of chloroplast 2-Cys Prx is shown.

Key words: Chloroplast, cyclophilin, decamer, hydrogen peroxide, peroxidase, peroxiredoxin, Pisum sativum, thioredoxin


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