title: Co-ordinated gene expression of photosynthetic glyceraldehyde-3-phosphate dehydrogenase, phosphoribulokinase, and CP12 in Arabidopsis thaliana.
abstract: Photosynthetic glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoribulokinase (PRK) interact in the chloroplast stroma through the action of the small peptide CP12. This supramolecular complex concurs with the light-dependent modulation in vivo of GAPDH and PRK activities. The expression patterns of several genes potentially involved in the formation of the complex have been studied. The genome of Arabidopsis thaliana includes seven genes for phosphorylating GAPDH isozymes, one PRK gene, and three genes for CP12. The expression of four GAPDH genes was analysed, i.e. GapA-1 and GapB for photosynthetic GAPDH of chloroplasts (NAD(P)-dependent), GapC-1 for cytosolic GAPDH, and GapCp-1 for plastid GAPDH (both NAD-dependent). A similar analysis was performed with PRK and two CP12 genes (CP12-1, CP12-2). The expression of GapA-1, GapB, PRK, and CP12-2 was found to be co-ordinately regulated with the same organ specificity, all four genes being mostly expressed in leaves and flower stalks, less expressed in flowers, and little or not expressed in roots and siliques. The expression of all these genes in leaves was terminated during prolonged darkness or following sucrose treatments, and their transcripts decayed with similar kinetics. At variance with CP12-2, gene CP12-1 appeared to be expressed more in flowers, it was totally insensitive to darkness, and less affected by sucrose. The expression of glycolytic GapC was strong and ubiquitous, insensitive to dark treatments, and unaffected by sucrose. GapCp transcripts were also found to be ubiquitous at lower levels, slowly decreasing in the dark and stable in sucrose-treated leaves. The co-ordinated expression of genes GapA-1, GapB, PRK, and CP12-2 is consistent with their specific involvement in the formation of the photosynthetic regulatory complex of chloroplasts.
authors.affiliation: Laboratory of Molecular Plant Physiology, Department of Biology, University of Bologna, Via Irnerio 42, I-40126 Bologna, Italy.
authors.forename: Lucia
authors.initials: L
authors.lastname: Marri
authors.forename: Francesca
authors.initials: F
authors.lastname: Sparla
authors.forename: Paolo
authors.initials: P
authors.lastname: Pupillo
authors.forename: Paolo
authors.initials: P
authors.lastname: Trost
mesh_terms: D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism*; D018506:Gene Expression Regulation, Plant / Q000187:drug effects / Q000502:physiology*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000096:biosynthesis* / Q000235:genetics; D008027:Light; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000096:biosynthesis* / Q000235:genetics; D010788:Photosynthesis / Q000235:genetics; D010940:Plant Proteins / Q000096:biosynthesis* / Q000235:genetics; D013395:Sucrose / Q000494:pharmacology
chemical_list: D010940:Plant Proteins; D013395:Sucrose; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D017853:Phosphotransferases (Alcohol Group Acceptor); C022390:phosphoribulokinase