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Journal of Bacteriology, September 2002, p. 5194-5199, Vol. 184, No. 18
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.18.5194-5199.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Staphylococcus aureus Contains Two Low-Molecular-Mass Phosphotyrosine Protein Phosphatases

Didier Soulat,1 Elisabeth Vaganay,1 Bertrand Duclos,1 Anne-Laure Genestier,2 Jérôme Etienne,2 and Alain J. Cozzone1*

Institute of Biology and Chemistry of Proteins, University of Lyon, CNRS,1 Department of Medical and Molecular Microbiology, Faculty of Medicine Laënnec, Lyon, France2

Received 27 March 2002/ Accepted 13 June 2002

The analysis of the different amino acid sequences deduced from the complete genome sequence of the gram-positive bacterium Staphylococcus aureus suggested the presence of two eukaryotic-protein-like low-molecular-mass phosphotyrosine protein phosphatases, which are usually found in gram-negative bacteria. To check this prediction, the corresponding genes were cloned and overexpressed in an Escherichia coli system. Two distinct proteins with an apparent molecular mass of 23 kDa each, PtpA and PtpB, were produced and then purified by affinity chromatography and assayed for enzymatic properties. As expected, they both exhibited phosphatase activity in vitro, with a maximum value at a pH of around 6.2 and at a temperature of 40°C. In addition, their kinetic constants, their specificity for phosphotyrosine residues, and their sensitivity to two phosphatase inhibitors, N-ethylmaleimide and orthovanadate, matched those of acid low-molecular-mass phosphotyrosine protein phosphatases.

* Corresponding author. Mailing address: Institute of Biology and Chemistry of Proteins, 7 Passage du Vercors, 69367 Lyon Cedex 07, France. Phone: 33 (0)4.72.72.26.72. Fax: 33 (0)4.72.72.26.01. E-mail: aj.cozzone{at}ibcp.fr.

Journal of Bacteriology, September 2002, p. 5194-5199, Vol. 184, No. 18
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.18.5194-5199.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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