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Analysis of the Molecular Evolutionary History of the Ascorbate Peroxidase Gene Family: Inferences from the Rice Genome

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Abstract

Ascorbate peroxidase (APx) is a class I peroxidase that catalyzes the conversion of H2O2 to H2O and O2 using ascorbate as the specific electron donor. This enzyme has a key function in scavenging reactive oxygen species (ROS) and the protection against toxic effects of ROS in higher plants, algae, and Euglena. Here we report the identification of an APx multigene family in rice and propose a molecular evolutionary relationship between the diverse APx isoforms. In rice, the APx gene family has eight members, which encode two cytosolic, two putative peroxisomal, and four chloroplastic isoforms, respectively. Phylogenetic analyses were conducted using all APx protein sequences available in the NCBI databases. The results indicate that the different APx isoforms arose by a complex evolutionary process involving several gene duplications. The structural organization of APx genes also reflects this process and provides evidence for a close relationship among proteins located in the same subcellular compartment. A molecular evolutionary pathway, in which cytosolic and peroxisomal isoforms diverged early from chloroplastic ones, is proposed.

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Acknowledgments

We gratefully acknowledge Dr. Jean Finnegan for critically reading the manuscript. We also thank Drs. Claudia Russo, Carlos E. Guerra Schrago, and Leonardo Karam Teixeira for helpful discussions and suggestions. This work was supported by FAPERJ, CNPq, and CAPES.

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Correspondence to Márcia Margis-Pinheiro.

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Reviewing Editor: Dr. Niles Lehman

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Teixeira, F.K., Menezes-Benavente, L., Margis, R. et al. Analysis of the Molecular Evolutionary History of the Ascorbate Peroxidase Gene Family: Inferences from the Rice Genome. J Mol Evol 59, 761–770 (2004). https://doi.org/10.1007/s00239-004-2666-z

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  • DOI: https://doi.org/10.1007/s00239-004-2666-z

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