Phosphorylation of Mycoplasma pneumoniae cytadherence-accessory proteins in cell extracts.
A cell-free system was used to characterize the phosphorylation of Mycoplasma pneumoniae proteins HMW1 and HMW2, which are involved in the adherence of this organism to human tracheal epithelium during infection. The pH and cation requirements for phosphorylation of HMW1 and HMW2 were determined, and the effects of glycolytic intermediates, cyclic AMP, and eukaryotic kinase-phosphatase inhibitors and stimulators on this process were examined. Phosphoamino acid analysis identified serine as the major phosphate acceptor for both HMW1 and HMW2 in this system.
Krebes
K A
KA
Department of Microbiology, University of Georgia, Athens 30602, USA.
Dirksen
L B
LB
Krause
D C
DC
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D002412:Cations / Q000378:metabolism; D015815:Cell Adhesion Molecules / Q000737:chemistry / Q000378:metabolism*; D002474:Cell-Free System; D000242:Cyclic AMP / Q000378:metabolism; D004789:Enzyme Activation; D004791:Enzyme Inhibitors; D006019:Glycolysis; D006863:Hydrogen-Ion Concentration; D009177:Mycoplasma pneumoniae / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D010766:Phosphorylation; D010770:Phosphotransferases / Q000378:metabolism; D012694:Serine / Q000378:metabolism
D001426:Bacterial Proteins; D002412:Cations; D015815:Cell Adhesion Molecules; D004791:Enzyme Inhibitors; D012694:Serine; D000242:Cyclic AMP; D010770:Phosphotransferases; D010744:Phosphoric Monoester Hydrolases