JXB Advance Access published online on February 13, 2004
Journal of Experimental Botany, doi:10.1093/jxb/erh079
© 2004 by Oxford University Press
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1 Institute for Biology I, Aachen University, Worringer Weg 1, D-52056 Aachen, Germany
* To whom correspondence should be addressed. E-mail: cp{at}bio1.rwth-aachen.de.
The fixation of molecular O2 by the oxygenase activity of Rubisco leads to the formation of phosphoglycolate in the chloroplast that is further metabolized in the process of photorespiration. The initial step of this pathway is the oxidation of glycolate to glyoxylate. Whereas in higher plants this reaction takes place in peroxisomes and is dependent on oxygen as a co-factor, most algae oxidize glycolate in the mitochondria using organic co-factors. The identification and characterization of a novel glycolate dehydrogenase in Arabidopsis thaliana is reported here. The enzyme is dependent on organic co-factors and resembles algal glycolate dehydrogenases in its enzymatic properties. Mutants of E. coli incapable of glycolate oxidation can be complemented by overexpression of the Arabidopsis open reading frame. The corresponding RNA accumulates preferentially in illuminated leaves, but was also found in other tissues investigated. A fusion of the N-terminal part of the Arabidopsis glycolate dehydrogenase to red fluorescent protein accumulates in mitochondria when overexpressed in the homologous system. Based on these results it is proposed that the basic photorespiratory system of algae is conserved in higher plants.
© 2004 Society for Experimental Biology
Research paper
A glycolate dehydrogenase in the mitochondria of Arabidopsis thaliana
2 Fraunhofer Institute of Molecular Biology and Applied Ecology, D-52074 Aachen, Germany
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