In vitro characterization of the Bacillus subtilis protein tyrosine phosphatase YwqE.
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.
Mijakovic
Ivan
I
Microbial Physiology and Genetics Group, BioCentrum, Technical University of Denmark, Lyngby, Denmark.
Musumeci
Lucia
L
Tautz
Lutz
L
Petranovic
Dina
D
Edwards
Robert A
RA
Jensen
Peter Ruhdal
PR
Mustelin
Tomas
T
Deutscher
Josef
J
Bottini
Nunzio
N
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics*; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010766:Phosphorylation; D017027:Protein Tyrosine Phosphatases / Q000235:genetics* / Q000378:metabolism*; D013379:Substrate Specificity
D017027:Protein Tyrosine Phosphatases