caa a22 4500 467894345 CHVBK 20180406152758.0 cr unu---uuuuu 170328e20060801xx s 000 0 eng 10.1007/s11103-006-0060-5 doi (NATIONALLICENCE)springer-10.1007/s11103-006-0060-5 Characterization of an Arabidopsis thaliana mutant lacking a cytosolic non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase [Elektronische Daten] [Sebastián Rius, Paula Casati, Alberto Iglesias, Diego Gomez-Casati] Non-phosphorylating glyceraldehyde- 3-phosphate dehydrogenase (NP-GAPDH) is a conserved cytosolic protein found in higher plants. In photosynthetic cells, the enzyme is involved in a shuttle transfer mechanism to export NADPH from the chloroplast to the cytosol. To investigate the role of this enzyme in plant tissues, we characterized a mutant from Arabidopsis thaliana having an insertion at the NP-GAPDH gene locus. The homozygous mutant was determined to be null respect to NP-GAPDH, as it exhibited undetectable levels of both transcription of NP-GAPDH mRNA, protein expression and enzyme activity. Transcriptome analysis demonstrated that the insertion mutant plant shows altered expression of several enzymes involved in carbohydrate metabolism. Significantly, cytosolic phosphorylating (NAD-dependent) glyceraldehyde-3-phosphate dehydrogenase mRNA levels are induced in the mutant, which correlates with an increase in enzyme activity. mRNA levels and enzymatic activity of glucose-6-phosphate dehydrogenase were also elevated, correlating with an increase in NADPH concentration. Moreover, increased ROS levels were measured in the mutant plants. Down-regulation of several glycolytic and photosynthetic genes suggests that NP-GAPDH is important for the efficiency of both metabolic processes. The results presented demonstrate that NP-GAPDH has a relevant role in plant growth and development. Springer Science+Business Media B.V., 2006 Glyceraldehydes-3-P dehydrogenase nationallicence Plant glycolysis nationallicence Arabidopsis nationallicence Rius Sebastián IIB-INTECH, UNSAM-CONICET, CC 164 (7130), Chascomús, Argentina aut Casati Paula Centro de Estudios Fotosintéticos y Bioquímicos (CEFOBI), Universidad Nacional de Rosario, Suipacha 531, 2000, Rosario, Argentina aut Iglesias Alberto Laboratorio de Enzimología Molecular, Facultad de Bioquímica y Ciencias Biológicas, Universidad Nacional del Litoral, Paraje "El Pozo”, CC 242, S3000ZAA, Santa Fe, Argentina aut Gomez-Casati Diego IIB-INTECH, UNSAM-CONICET, CC 164 (7130), Chascomús, Argentina aut Plant Molecular Biology Kluwer Academic Publishers 61/6(2006-08-01), 945-957 0167-4412 61:6<945 2006 61 11103 https://doi.org/10.1007/s11103-006-0060-5 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s11103-006-0060-5 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Rius Sebastián IIB-INTECH, UNSAM-CONICET, CC 164 (7130), Chascomús, Argentina aut NATIONALLICENCE 700 1- Casati Paula Centro de Estudios Fotosintéticos y Bioquímicos (CEFOBI), Universidad Nacional de Rosario, Suipacha 531, 2000, Rosario, Argentina aut NATIONALLICENCE 700 1- Iglesias Alberto Laboratorio de Enzimología Molecular, Facultad de Bioquímica y Ciencias Biológicas, Universidad Nacional del Litoral, Paraje "El Pozo”, CC 242, S3000ZAA, Santa Fe, Argentina aut NATIONALLICENCE 700 1- Gomez-Casati Diego IIB-INTECH, UNSAM-CONICET, CC 164 (7130), Chascomús, Argentina aut NATIONALLICENCE 773 0- Plant Molecular Biology Kluwer Academic Publishers 61/6(2006-08-01), 945-957 0167-4412 61:6<945 2006 61 11103 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer