ArticleJournal of bacteriology1999
Cells of Escherichia coli contain a protein-tyrosine kinase, Wzc, and a phosphotyrosine-protein phosphatase, Wzb.
Article in Journal of bacteriology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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52 citing papers in PubMed, 161 citations in OpenAlex.
- Study of Stress Granule Core Protein AtUBP1b PhosphorylationPlants (Basel, Switzerland) · 2025Article
- Identification of EcpK, a bacterial tyrosine pseudokinase important for exopolysaccharide biosynthesis inJournal of bacteriology · 2025Article
- Reverse-Phase Protein Microarrays for OverexpressedAnalytical chemistry · 2024Article
- Characteristics ofFrontiers in cellular and infection microbiology · 2023Article
- Structural basis for the recognition of the bacterial tyrosine kinase Wzc by its cognate tyrosine phosphatase Wzb.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Tyrosine phosphorylation-dependent localization of TmaR that controls activity of a major bacterial sugar regulator by polar sequestration.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The Tyrosine-Autokinase UbK Is Required for Proper Cell Growth and Cell Morphology ofFrontiers in microbiology · 2019Article
- Tyrosine Phosphorylation and Dephosphorylation in Burkholderia cenocepacia Affect Biofilm Formation, Growth under Nutritional Deprivation, and Pathogenicity.Applied and environmental microbiology · 2016Article
- New potential eukaryotic substrates of the mycobacterial protein tyrosine phosphatase PtpA: hints of a bacterial modulation of macrophage bioenergetics state.Scientific reports · 2015Article
- Protein-tyrosine phosphorylation in Bacillus subtilis: a 10-year retrospective.Frontiers in microbiology · 2015Article
- Biomolecular Mechanisms of Pseudomonas aeruginosa and Escherichia coli Biofilm Formation.Pathogens (Basel, Switzerland) · 2014Review
- The role of bacterial protein tyrosine phosphatases in the regulation of the biosynthesis of secreted polysaccharides.Antioxidants & redox signaling · 2014Review
- Microbial protein-tyrosine kinases.The Journal of biological chemistry · 2014Review
- Evolution of bacterial protein-tyrosine kinases and their relaxed specificity toward substrates.Genome biology and evolution · 2014Article
- The UDP-glucose dehydrogenase of Escherichia coli K-12 displays substrate inhibition by NAD that is relieved by nucleotide triphosphates.The Journal of biological chemistry · 2013Article
- Regulatory interactions between a bacterial tyrosine kinase and its cognate phosphatase.The Journal of biological chemistry · 2013Article
- Wzi is an outer membrane lectin that underpins group 1 capsule assembly in Escherichia coli.Structure (London, England : 1993) · 2013Article
- Bacterial tyrosine kinases: evolution, biological function and structural insights.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Tyrosine phosphorylation and bacterial virulence.International journal of oral science · 2012Review
- Chemical inhibition of bacterial protein tyrosine phosphatase suppresses capsule production.PloS one · 2012Article
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6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two proteins of Escherichia coli, termed Wzc and Wzb, were analyzed for their capacity to participate in the reversible phosphorylation of proteins on tyrosine. First, Wzc was overproduced from its specific gene and purified to homogeneity by affinity chromatography. Upon incubation in the presence of radioactive ATP, it was found to effectively autophosphorylate. Two-dimensional analysis of its phosphoamino acid content revealed that it was modified exclusively at tyrosine. Second, Wzb was also overproduced from the corresponding gene and purified to homogeneity by affinity chromatography. It was shown to contain a phosphatase activity capable of cleaving the synthetic substrate p-nitrophenyl phosphate into p-nitrophenol and free phosphate. In addition, it was assayed on individual phosphorylated amino acids and appeared to dephosphorylate specifically phosphotyrosine, with no effect on phosphoserine or phosphothreonine. Such specificity for phosphotyrosine was confirmed by the observation that Wzb was able to dephosphorylate previously autophosphorylated Wzc. Together, these data demonstrate, for the first time, that E. coli cells contain both a protein-tyrosine kinase and a phosphotyrosine-protein phosphatase. They also provide evidence that this phosphatase can utilize the kinase as an endogenous substrate, which suggests the occurrence of a regulatory mechanism connected with reversible protein phosphorylation on tyrosine. From comparative analysis of amino acid sequences, Wzc was found to be similar to a number of proteins present in other bacterial species which are all involved in the synthesis or export of exopolysaccharides. Since these polymers are considered important virulence factors, we suggest that reversible protein phosphorylation on tyrosine may be part of the cascade of reactions that determine the pathogenicity of bacteria.
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