In Vitro Characterization of the Bacillus subtilis Protein Tyrosine Phosphatase YwqE

Author:

Mijakovic Ivan12,Musumeci Lucia3,Tautz Lutz3,Petranovic Dina1,Edwards Robert A.34,Jensen Peter Ruhdal1,Mustelin Tomas3,Deutscher Josef2,Bottini Nunzio3

Affiliation:

1. Microbial Physiology and Genetics Group, BioCentrum, Technical University of Denmark, DK-2800 Lyngby, Denmark

2. Microbiologie et Génétique Moléculaire, CNRS/INRA/INA-PG, 78850 Thierval-Grignon, France

3. Inflammatory and Infectious Disease Center, The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, California 92037

4. Fellowship for the Interpretation of Genomes, Center for Microbial Sciences, San Diego State University, San Diego, California 92182

Abstract

ABSTRACT 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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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