JXB Advance Access originally published online on July 26, 2006
Journal of Experimental Botany 2006 57(12):3033-3042; doi:10.1093/jxb/erl060
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RESEARCH PAPER |
The Arabidopsis ascorbate peroxidase 3 is a peroxisomal membrane-bound antioxidant enzyme and is dispensable for Arabidopsis growth and development

1Department of Biological Sciences, Texas Tech University, Lubbock, TX 79409, USA
2Department of Crop Sciences, University of Illinois, Urbana, IL 61801, USA
To whom correspondence should be addressed. E-mail: hong.zhang{at}ttu.edu
Ascorbate peroxidase (APX) exists as several isoforms that are found in various compartments in plant cells. The cytosolic and chloroplast APXs appear to play important roles in antioxidation metabolism in plant cells, yet the function of peroxisomal APX is not well studied. In this study, the localization of a putative peroxisomal membrane-bound ascorbate peroxidase, APX3 from Arabidopsis, was confirmed by studying the green fluorescent protein (GFP)APX3 fusion protein in transgenic plants. GFPAPX3 was found to co-localize with a reporter protein that was targeted to peroxisomes by the peroxisomal targeting signal 1. The function of APX3 in Arabidopsis was investigated by analysing an APX3 knockout mutant under normal and several stress conditions. It was found that loss of function in APX3 does not affect Arabidopsis growth and development, suggesting that APX3 may not be an important antioxidant enzyme in Arabidopsis, at least under the conditions that were tested, or the function of APX3 could be compensated by other antioxidant enzymes in plant cells.
Key words: Antioxidation, hydrogen peroxide scavenging, peroxisomal membrane targeting, reactive oxygen species, subcellular localization
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