ArticlePloS one2011
Phosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by PknA and PknB.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 49 citations in OpenAlex.
- Mycobacterial PstP impairs host RNA alternative splicing by dephosphorylation of spliceosome RBMX at S189.iMetaOmics · 2025Article
- Giving a signal: how protein phosphorylation helps Bacillus navigate through different life stages.FEMS microbiology reviews · 2023Review
- Mycobacterial serine/threonine phosphatase PstP is phosphoregulated and localized to mediate control of cell wall metabolism.Molecular microbiology · 2022Article
- The enterococcal PASTA kinase: A sentinel for cell envelope stress.Molecular oral microbiology · 2021Review
- Phosphorylation on PstP Regulates Cell Wall Metabolism and Antibiotic Tolerance in Mycobacterium smegmatis.Journal of bacteriology · 2021Article
- Mycobacterial phosphatase PstP regulates global serine threonine phosphorylation and cell division.Scientific reports · 2019Article
- Inhibition of the Protein Phosphatase CppA Alters Development of Chlamydia trachomatis.Journal of bacteriology · 2018Article
- Identification and Biochemical Characterization of a Novel Protein Phosphatase 2C-Like Ser/Thr Phosphatase in Escherichia coli.Journal of bacteriology · 2018Article
- Identification of Novel Physiological Substrates ofMolecular & cellular proteomics : MCP · 2018Article
- The transpeptidase PbpA and noncanonical transglycosylase RodA ofThe Journal of biological chemistry · 2018Article
- Epigenetic Phosphorylation Control of Mycobacterium tuberculosis Infection and Persistence.Microbiology spectrum · 2017Review
- Ser/Thr protein kinase PrkC-mediated regulation of GroEL is critical for biofilm formation inNPJ biofilms and microbiomes · 2017Article
- Serine/Threonine Protein Phosphatase PstP of Mycobacterium tuberculosis Is Necessary for Accurate Cell Division and Survival of Pathogen.The Journal of biological chemistry · 2016Article
- Ser/Thr Phosphorylation Regulates the Fatty Acyl-AMP Ligase Activity of FadD32, an Essential Enzyme in Mycolic Acid Biosynthesis.The Journal of biological chemistry · 2016Article
- Systematic Analysis of Mycobacterial Acylation Reveals First Example of Acylation-mediated Regulation of Enzyme Activity of a Bacterial Phosphatase.The Journal of biological chemistry · 2015Article
- Mycobacterial Growth.Cold Spring Harbor perspectives in medicine · 2015Review
- Ser/Thr phosphorylation as a regulatory mechanism in bacteria.Current opinion in microbiology · 2015Review
- Comparative Ser/Thr/Tyr phosphoproteomics between two mycobacterial species: the fast growing Mycobacterium smegmatis and the slow growing Mycobacterium bovis BCG.Frontiers in microbiology · 2015Article
- Identification of Ser/Thr kinase and forkhead associated domains in Mycobacterium ulcerans: characterization of novel association between protein kinase Q and MupFHA.PLoS neglected tropical diseases · 2014Article
- Mycobacterium tuberculosis Serine/Threonine Protein Kinases.Microbiology spectrum · 2014Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe integrated functions of 11 Ser/Thr protein kinases (STPKs) and one phosphatase manipulate the phosphorylation levels of critical proteins in Mycobacterium tuberculosis. In this study, we show that the lone Ser/Thr phosphatase (PstP) is regulated through phosphorylation by STPKs. PRINCIPAL
findingsPstP is phosphorylated by PknA and PknB and phosphorylation is influenced by the presence of Zn(2+)-ions and inorganic phosphate (Pi). PstP is differentially phosphorylated on the cytosolic domain with Thr(137), Thr(141), Thr(174) and Thr(290) being the target residues of PknB while Thr(137) and Thr(174) are phosphorylated by PknA. The Mn(2+)-ion binding residues Asp(38) and Asp(229) are critical for the optimal activity of PstP and substitution of these residues affects its phosphorylation status. Native PstP and its phosphatase deficient mutant PstP(c) (D38G) are phosphorylated by PknA and PknB in E. coli and addition of Zn(2+)/Pi in the culture conditions affect the phosphorylation level of PstP. Interestingly, the phosphorylated phosphatase is more active than its unphosphorylated equivalent. CONCLUSIONS AND SIGNIFICANCE: This study establishes the novel mechanisms for regulation of mycobacterial Ser/Thr phosphatase. The results indicate that STPKs and PstP may regulate the signaling through mutually dependent mechanisms. Consequently, PstP phosphorylation may play a critical role in regulating its own activity. Since, the equilibrium between phosphorylated and non-phosphorylated states of mycobacterial proteins is still unexplained, understanding the regulation of PstP may help in deciphering the signal transduction pathways mediated by STPKs and the reversibility of the phenomena.
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