Phosphorylation of a 65 kDa cytoplasmic protein by the Escherichia coli YeaG kinase

Abstract

The Escherichia coli YeaG cytoplasmic protein, which is endowed with autokinase and casein kinase activities, has been shown to phosphorylate specifically a 65-kDa cytoplasmic protein. This protein cannot be phosphorylated in an extract from the yeaG mutant, but it can be phosphorylated in an extract from the parental strain or in mutant extract SUPPL.emented with purified YeaG. This phosphoprotein displays a pH of 6.8 in 2D gels. Stationary phase induction of YeaG correlates with a significant growth defect of the yeaG mutant at the end of the exponential phase. © Springer-Verlag and the University of Milan 2010.