Identification of Phosphorylation Sites Altering Pollen Soluble Inorganic Pyrophosphatase Activity

• Published in: Plant physiology (Bethesda) Vol. 173; no. 3; pp. 1606 - 1616
• Main Authors: Eaves, Deborah J., Haque, Tamanna, Tudor, Richard L., Barron, Yoshimi, Zampronio, Cleidiane G., Cotton, Nicholas P. J., de Graaf, Barend H. J., White, Scott A., Cooper, Helen J., Franklin, F. Christopher H., Harper, Jeffery F., Franklin-Tong, Vernonica E.
• Format: Journal Article
• Language: English
• Published: United States American Society of Plant Biologists 01.03.2017
• Subjects: Amino Acid Sequence; Base Sequence; Binding Sites - genetics; BIOCHEMISTRY AND METABOLISM; Calcium - metabolism; Calcium - pharmacology; Chromatography, Liquid; Electrophoresis, Polyacrylamide Gel; Hydrogen Peroxide - pharmacology; Hydrogen-Ion Concentration; Inorganic Pyrophosphatase - genetics; Inorganic Pyrophosphatase - metabolism; Isoenzymes - genetics; Isoenzymes - metabolism; Mutation; Oxidants - pharmacology; Papaver - enzymology; Papaver - genetics; Phosphorylation; Phylogeny; Plant Proteins - genetics; Plant Proteins - metabolism; Pollen - enzymology; Pollen - genetics; Protein Kinases - classification; Protein Kinases - genetics; Protein Kinases - metabolism; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid; Solubility; Substrate Specificity; Tandem Mass Spectrometry

Protein phosphorylation regulates numerous cellular processes. Identifying the substrates and protein kinases involved is vital to understand how these important posttranslational modifications modulate biological function in eukaryotic cells. Pyrophosphatases catalyze the hydrolysis of inorganic ph...