New insights into plant transaldolase.
The oxidative pentose phosphate pathway (OPPP) provides plants with important substrates for both primary and secondary metabolism via the oxidation of glucose-6-phosphate. The OPPP is also thought to generate large amounts of reducing power to drive various anabolic processes. In animals this major pathway is located within the cytoplasm of cells, but in plants its subcellular compartmentation is far from clear. Although several enzymes of the OPPP were demonstrated to have both cytosolic and plastidic counterparts, there is yet no evidence for a full set of functional enzymes in each compartment. We report here the isolation of two coding sequences from tomato (Lycopersicon esculentum L.) which encode phylogenetically distant sequences (ToTal1 and ToTal2) that putatively encode distinct plastidic TA isoforms. The kinetic characterization of ToTal1 revealed that, unlike other enzymes of the non-oxidative branch of the OPPP, ToTal1 does not follow a Michaelis-Menten mode of catalysis which has implications for its role in regulating carbon flux between primary and secondary metabolism. TA genes appear to be differentially regulated at the level of gene expression in plant tissues and in response to environmental factors which suggests that TA isoforms have a non-overlapping role for plant metabolism.
Caillau
Maxime
M
Department of Animal and Plant Sciences, University of Sheffield, Sheffield S102TN, UK.
Paul Quick
W
W
D000595:Amino Acid Sequence; D002874:Chromosome Mapping; D032461:Chromosomes, Plant; D018506:Gene Expression Regulation, Plant; D007527:Isoenzymes; D007700:Kinetics; D018551:Solanum lycopersicum / Q000201:enzymology* / Q000235:genetics*; D008969:Molecular Sequence Data; D010427:Pentose Phosphate Pathway; D010802:Phylogeny; D010940:Plant Proteins; D017386:Sequence Homology, Amino Acid; D014153:Transaldolase / Q000235:genetics* / Q000378:metabolism*
D007527:Isoenzymes; D010940:Plant Proteins; D014153:Transaldolase