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Type: Journal article
Title: In vitro characterization and identification of potential substrates of a low molecular weight protein tyrosine phosphatase in Streptococcus pneumoniae
Author: Ahmad, Z.
Morona, R.
Standish, A.
Citation: Microbiology, 2018; 164(4):697-703
Publisher: Microbiology Society
Issue Date: 2018
ISSN: 1350-0872
Statement of
Zuleeza Ahmad, Renato Morona and Alistair J. Standish
Abstract: Streptococcus pneumoniae is a major human pathogen responsible for significant mortality and morbidity worldwide. Within the annotated genome of the pneumococcus lies a previously uncharacterized protein tyrosine phosphatase which shows homology to low molecular weight protein tyrosine phosphatases (LMWPTPs). LMWPTPs modulate many processes critical for the pathogenicity of a number of bacteria including capsular polysaccharide biosynthesis, stress response and persistence in host macrophages. Here, we demonstrate that Spd1837 is indeed a LMWPTP, by purifying the protein, and characterizing its phosphatase activity. Spd1837 showed specific tyrosine phosphatase activity, and it did not form higher order oligomers in contrast to many other LMWPTPs. Substrate-trapping assays using the wild-type and the phosphatase-deficient Spd1837 identified potential substrates/interacting proteins including major metabolic enzymes such as ATP-dependent-6-phosphofructokinase and Hpr kinase/phosphorylase. Given the tight association between the bacterial basic physiology and virulence, this study hopes to prompt further investigation of how the pneumococcus controls its metabolic flux via the LMWPTP Spd1837.
Keywords: Tyrosine phosphorylation; low molecular weight phosphatase; pneumococcus; Streptococcus pneumoniae; phosphatase substrates identification
Rights: © 2018 The Authors
DOI: 10.1099/mic.0.000631
Grant ID:
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Molecular and Biomedical Science publications

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