Tyrosine phosphatase TpbA controls rugose colony formation in Pseudomonas aeruginosa by dephosphorylating diguanylate cyclase TpbB.
Tyrosine phosphatase TpbA in Pseudomonas aeruginosa PA14 is a negative regulator of the diguanylate cyclase TpbB. Inactivation of TpbA caused rugose colony morphology which is related to cell persistence in clinical infections. We show here that TpbA is a dual specific tyrosine phosphatase, that TpbB is phosphorylated, and that TpbA controls phosphorylation of TpbB at both Tyr and Ser/Thr residues in vivo as detected by Western blot analysis. In addition, TpbB is demonstrated to be a substrate of TpbA in vitro using purified enzymes. Thus, TpbA controls the rugose morphology in P. aeruginosa by dephosphorylating TpbB.
Pu
Mingming
M
Department of Chemical Engineering, Texas A&M University, College Station, TX 77843-3122, United States.
Wood
Thomas K
TK
D029968:Escherichia coli Proteins; D019761:Phosphorus-Oxygen Lyases / Q000378:metabolism*; D010766:Phosphorylation; D017027:Protein Tyrosine Phosphatases / Q000235:genetics / Q000378:metabolism*; D011550:Pseudomonas aeruginosa / Q000166:cytology* / Q000201:enzymology / Q000254:growth & development; D013379:Substrate Specificity
D029968:Escherichia coli Proteins; D017027:Protein Tyrosine Phosphatases; D019761:Phosphorus-Oxygen Lyases; C060720:diguanylate cyclase