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Journal of Bacteriology, October 2000, p. 5634-5638, Vol. 182, No. 19
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Characterization of PrpC from Bacillus subtilis, a Member of the PPM Phosphatase Family

M. Obuchowski,1,dagger E. Madec,1 D. Delattre,1 G. Boël,1,Dagger A. Iwanicki,1,dagger D. Foulger,2,§ and S. J. Séror1,*

Institut de Génétique et Microbiologie, UMR CNRS 8621, Université Paris-Sud, 91405 Orsay Cedex, France,1 and Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, United Kingdom2

Received 13 April 2000/Accepted 29 June 2000

We cloned the yloO gene and purified a His-tagged form of its product, the putative protein phosphatase YloO, which we now designate PrpC. This closely resembles the human protein phosphatase PP2C, a member of the PPM family, in sequence and predicted secondary structure. PrpC has phosphatase activity in vitro against a synthetic substrate, p-nitrophenol phosphate, and endogenous Bacillus subtilis proteins. The prkC and prpC genes are adjacent on the chromosome, and the phosphorylated form of PrkC is a substrate for PrpC. These findings suggest that PrkC and PrpC may function as a couple in vivo.

* Corresponding author. Mailing address: Institut de Génétique et Microbiologie, UMR CNRS 8621, Université Paris-Sud, Bât. 409, 91405 Orsay Cedex, France. Phone: (33) 1 69 15 57 14. Fax: (33) 1 69 15 78 08. E-mail: seror{at}igmors.u-psud.fr.

dagger Present address: Department of Molecular Biology, University of Gdansk, 80-822 Gdansk, Poland.

Dagger Present address: INRA-CNRS, F78850 Thiverval-Grignon, France.

§ Present address: Department of Plant Sciences, University of Oxford, Oxford, United Kingdom.

Journal of Bacteriology, October 2000, p. 5634-5638, Vol. 182, No. 19
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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