Protein phosphorylation in Mycoplasma gallisepticum
- 1 September 1988
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 176 (1), 61-67
- https://doi.org/10.1111/j.1432-1033.1988.tb14251.x
Abstract
Incubation of the soluble fraction derived from Mycoplasma gallisepticum cells with [.gamma.-32P]ATP results in the phosphorylation of several endogenous proteins. One protein with an apparent molecular mass of 55 kDa was the acceptor of more than 95% of the radioactive phosphate. This protein was also found to be radiolabeled in intact cells grown in the presence of [32P]orthophosphate. Acid hydrolysis of the phosphorylated 55-kDa protein followed by two-dimensional electrophoresis revealed that the 32P-labeled material co-migrated with phosphoserine. The in vitro phosphorylation of the 55-kDa protein has an optimum pH of 5.5-6.0 and is not affected by various metabolites of glycolysis, by cAMP or by calmodulin with or without Ca2+. The phosphorylation is dependent upon divalent cations, a dependency that is best fulfilled by the simultaneous addition of Ca2+ and Zn2+ that act in a specific and cooperative manner. Of a variety of possible exogenous protein acceptors tested, the endogenous protein kinase was capable to phosphorylate only phosvitin. The phosphorylation of the 55-kDa protein is reversible through the activity of a phosphoprotein phosphatase present in the soluble fraction of M. gallisepticum. The phosphoprotein phosphatase has an optimum pH of 7.5-8.0, is inhibited by NaF and stimulated to a large extent by inorganic phosphate and arsenate and to a lesser extent by pyrophosphate ATP and ADP. The possible association of the reversible protein phosphorylation to cell shape and gliding motility of M. gallisepticum are discussed.This publication has 34 references indexed in Scilit:
- Characterization of the phosphoproteins of Escherichia coli cells by electrophoretic analysisEuropean Journal of Biochemistry, 1986
- Protein phosphorylation in bacteriaTrends in Biochemical Sciences, 1984
- Filamentous structures in adherent Mycoplasma pneumoniae cells treated with nonionic detergents.The Journal of cell biology, 1981
- Membrane lipids of Mycoplasma gallisepticum: a disaturated phosphatidylcholine and a phosphatidylglycerol with an unusual positional distribution of fatty acidsBiochemistry, 1979
- Phosphorylation-Dephosphorylation of EnzymesAnnual Review of Biochemistry, 1979
- Gliding mycoplasmas are inhibited by cytochalasin B and contain a polymerizable protein fractionJournal of Supramolecular Structure, 1979
- Dephosphorylation of human erythrocyte membranes induced by Sendai virusBiochemistry, 1977
- Isolation and Characterization of a Non-Helical Strain of Spiroplasma citriJournal of General Microbiology, 1977
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970