Association of L-galactone-1,4-lactone dehydrogenase with other mitochondrial proteins

GERGOFF GROZEFF, GUSTAVO; BARTOLI, CARLOS GUILLERMO; CÓRDOBA, JUAN PABLO; ZABALETA, EDUARDO; BRAUN, HANS-PETER

Rosario

Congreso; 8th International Conference for Plant Mitochondria Biology; 2013

Ascorbic acid (AA, Vitamin C) constitutes one of the most important soluble antioxidants in plants. It is also necessary for human diet, due to a mutation in the last enzyme of the synthesis pathway. In plants, its synthesis is part of an interconnected network, where the mitochondrial L-galactone-1,4-lactone dehydrogenase (GLDH) catalyzes the last reaction. The regulation of the synthesis pathway and, in particular GLDH activity, is still unknown and it does not depend on the amount of the GLDH protein. The aim of this project is to study the association of GLDH with other mitochondrial proteins that possibly regulate AA formation. We transformed Arabidopsis plants with a 35S::GLDH::c-myc construct which overexpress the fusion protein GLDH-c-myc to identify the mitochondrial proteins that interact with GLDH. At this point of the work we have identified overexpressed lines by western blot. The next objective is to obtain the proteins interacting with GLDH through a reversible crosslinker column using an anti-c-myc. The proteins eluted from the columns will be separated on gels and identified by mass spectrometry. These results are expected to give important information of the processes that modify the synthesis and accumulation of AA in edible plant organs.