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Published on April 4, 2008; 10.1104/pp.107.110247

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Received October 1, 2007
Accepted March 20, 2008

AtOSA1 a member of Abc1-like family as a new factor in cadmium and oxidative stress response

Michal Jasinski , Damien Sudre , Gert Schansker , Maya Schellenberg , Signarbieux Constant , Enrico Martinoia , and Lucien Bovet *

University of Zurich, Institute of Plant Biology, Zollikerstrasse 107, 8008 Zurich, Switzerland; University of Bern, IPS-Plant nutrition, Altenbergrain 21, 3012 Bern, Switzerland; University of Geneva, Bioenergetics Laboratory, Chemin des Embrouchis 10, 1254 Jussy/Lullier, Switzerland; University of Fribourg, Department of Biology - Plant Biology, rue Albert Gockel 3, 1700 Fribourg, Switzerland; Institute of Bioorganic Chemistry, Polish Academy of Sciences, Noskowskiego 12/14, 61-704 Poznan, Poland

* Corresponding author; email: lucien.bovet{at}pmintl.com.

The analysis of gene expression in Arabidopsis thaliana using cDNA-microarrays and RT-PCR showed that AtOSA1 (Arabidopsis thaliana Oxidative Stress related Abc1 like protein) transcript levels are influenced by Cd2+ treatment. The comparison of protein sequences revealed that AtOSA1 belongs to the family of Abc1 proteins. Up to now, Abc1-like proteins have been identified in prokaryotes and in the mitochondria of eukaryotes. AtOSA1 is the first member of this family to be localized in the chloroplasts. However, despite sharing homology to the mitochondrial ABC1 of Saccharomyces cerevisiae, AtOSA1 was not able to complement yeast strains deleted in endogenous ABC1 gene, thereby suggesting different function between AtOSA1 and the yeast ABC1.

The atosa1-1 and atosa1-2 T-DNA insertion mutants were more affected than wild type plants by Cd2+ and revealed an increased sensitivity towards oxidative stress (H2O2) and high light. The mutants exhibited higher superoxide dismutase activities and differences in the expression of genes involved in the antioxidant pathway.

In addition to the conserved Abc1 region in the AtOSA1 protein sequence, putative kinase domains were found. Protein kinase assays in gelo using myelin basic protein as a kinase substrate revealed that chloroplast envelope membrane fractions from the AtOSA1 mutant lacked a 70 kD phosphorylated protein compared to the wild type. Our data suggest that the chloroplast AtOSA1 protein is a new factor playing a role in a balance of oxidative stress.






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