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Journal of Bacteriology, May 2005, p. 3384-3390, Vol. 187, No. 10
0021-9193/05/$08.00+0     doi:10.1128/JB.187.10.3384-3390.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

In Vitro Characterization of the Bacillus subtilis Protein Tyrosine Phosphatase YwqE

Ivan Mijakovic,^1,3 Lucia Musumeci,^2, Lutz Tautz,^2, Dina Petranovic,¹ Robert A. Edwards,^2,4 Peter Ruhdal Jensen,¹ Tomas Mustelin,² Josef Deutscher,³ and Nunzio Bottini^2*

Microbial Physiology and Genetics Group, BioCentrum, Technical University of Denmark, DK-2800 Lyngby, Denmark,¹ Inflammatory and Infectious Disease Center, The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, California 92037,² Microbiologie et Génétique Moléculaire, CNRS/INRA/INA-PG, 78850 Thierval-Grignon, France,³ Fellowship for the Interpretation of Genomes, Center for Microbial Sciences, San Diego State University, San Diego, California 92182⁴

Received 14 December 2004/ Accepted 2 February 2005

Both gram-negative and gram-positive bacteria possess protein tyrosine phosphatases (PTPs) with a catalytic Cys residue. In addition, many gram-positive bacteria have acquired a new family of PTPs, whose first characterized member was CpsB from Streptococcus pneumoniae. Bacillus subtilis contains one such CpsB-like PTP, YwqE, in addition to two class II Cys-based PTPs, YwlE and YfkJ. The substrates for both YwlE and YfkJ are presently unknown, while YwqE was shown to dephosphorylate two phosphotyrosine-containing proteins implicated in UDP-glucuronate biosynthesis, YwqD and YwqF. In this study, we characterize YwqE, compare the activities of the three B. subtilis PTPs (YwqE, YwlE, and YfkJ), and demonstrate that the two B. subtilis class II PTPs do not dephosphorylate the physiological substrates of YwqE.

These two authors contributed equally to this study.

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