One of two different ADP-glucose pyrophosphorylase genes from potato responds strongly to elevated levels of sucrose

• Published in: Molecular & general genetics Vol. 224; no. 1; p. 136
• Main Authors: Müller-Röber, B T, Kossmann, J, Hannah, L C, Willmitzer, L, Sonnewald, U
• Format: Journal Article
• Language: English
• Published: Germany 01-10-1990
• Subjects: Amino Acid Sequence; Base Sequence; Blotting, Northern; Cloning, Molecular; DNA - isolation & purification; Edetic Acid - pharmacology; Gene Expression Regulation; Genes, Plant; Glucose-1-Phosphate Adenylyltransferase; Molecular Sequence Data; Nucleotidyltransferases - genetics; Nucleotidyltransferases - metabolism; RNA - metabolism; Sequence Homology, Nucleic Acid; Solanum tuberosum - enzymology; Solanum tuberosum - genetics; Sorbitol - pharmacology; Sucrose - pharmacology; Transcription, Genetic
• ISSN: 0026-8925
• DOI: 10.1007/bf00259460

The key regulatory step in starch biosynthesis is catalyzed by the tetrameric enzyme ADP-glucose pyrophosphorylase (AGPase). In leaf and storage tissue, the enzyme catalyzes the synthesis of ADP-glucose from glucose-1-phosphate and ATP. Using heterologous probes from maize, two sets (B and S) of cDNA clones encoding potato AGPase were isolated from a tuberspecific cDNA library. Sequence analysis revealed homology to other plant and bacterial sequences. Transcript sizes are 1.9 kb (AGPase B) and 2.1 kb (AGPase S). Northern blot experiments show that the two genes differ in their expression patterns in different organs. Furthermore, one of the genes (AGPase S) is strongly inducible by metabolizable carbohydrates (e.g. sucrose) at the RNA level. The accumulation of AGPase S mRNA was always found to be accompanied by an increase in starch content. This suggests a link between AGPase S expression and the status of a tissue as either a sink for or a source of carbohydrates. By contrast, expression of AGPase B is much less variable under various experimental conditions.