ArticleJournal of bacteriology2006
The Ser/Thr protein kinase PknB is essential for sustaining mycobacterial growth.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.
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Who cites it
86 citing papers in PubMed, 194 citations in OpenAlex.
- Structural Modification of Indole Derivatives as PknB Inhibitors for Enhanced Enzymatic Inhibition and Antimycobacterial Activity.ACS omega · 2026Article
- Multifaceted Small Molecules as Enzyme Modulators: Cases of Drug Discovery/Repurposing Illustrating Nature's Pragmatism.BioMed research international · 2026Review
- An atlas of bacterial serine-threonine kinases reveals functional diversity and key distinctions from eukaryotic kinases.Science signaling · 2025Article
- Article
- Identification of Anti-Tuberculosis Drugs Targeting DNA Gyrase A and Serine/Threonine Protein Kinase PknB: A Machine Learning-Assisted Drug-Repurposing Approach.Tropical medicine and infectious disease · 2024Article
- Experimental measurement and computational prediction of bacterial Hanks-type Ser/Thr signaling system regulatory targets.Molecular microbiology · 2024Review
- Resuscitation Promotion Factor: A Pronounced Bacterial Cytokine in Propelling Bacterial Resuscitation.Microorganisms · 2024Review
- OrthoRefine: automated enhancement of prior ortholog identification via synteny.BMC bioinformatics · 2024Article
- The Antitubercular Activities of Natural Products with Fused-Nitrogen-Containing Heterocycles.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Polypharmacology-Driven Discovery and Design of Highly Selective, Dual and Multitargeting Inhibitors ofCurrent drug targets · 2024Review
- Role of serine/threonine protein phosphatase PrpN in the life cycle of Bacillus anthracis.PLoS pathogens · 2022Article
- PeSTK db a comprehensive data repository of Probiotic Serine Threonine kinases.Scientific data · 2022Article
- Mycobacterium tuberculosis PknK Substrate Profiling Reveals Essential Transcription Terminator Protein Rho and Two-Component Response Regulators PrrA and MtrA as Novel Targets for Phosphorylation.Microbiology spectrum · 2022Article
- Inhibitors targeting the autophosphorylation of serine/threonine kinase ofFrontiers in microbiology · 2022Article
- In Silico Identification of Possible Inhibitors for Protein Kinase B (PknB) ofMolecules (Basel, Switzerland) · 2021Article
- Xenogeneic silencing relies on temperature-dependent phosphorylation of the host H-NS protein in Shewanella.Nucleic acids research · 2021Article
- 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
- Probing the Highly Disparate Dual Inhibitory Mechanisms of Novel Quinazoline Derivatives againstMolecules (Basel, Switzerland) · 2020Article
- Phosphoproteomic Approaches to Discover Novel Substrates of Mycobacterial Ser/Thr Protein Kinases.Molecular & cellular proteomics : MCP · 2020Review
26 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The receptor-like protein kinase PknB from Mycobacterium tuberculosis is encoded by the distal gene in a highly conserved operon, present in all actinobacteria, that may control cell shape and cell division. Genes coding for a PknB-like protein kinase are also found in many more distantly related gram-positive bacteria. Here, we report that the pknB gene can be disrupted by allelic replacement in M. tuberculosis and the saprophyte Mycobacterium smegmatis only in the presence of a second functional copy of the gene. We also demonstrate that eukaryotic Ser/Thr protein kinase inhibitors, which inactivate PknB in vitro with a 50% inhibitory concentration in the submicromolar range, are able to kill M. tuberculosis H37Rv, M. smegmatis mc(2)155, and Mycobacterium aurum A+ with MICs in the micromolar range. Furthermore, significantly higher concentrations of these compounds are required to inhibit growth of M. smegmatis strains overexpressing PknB, suggesting that this protein kinase is the molecular target. These findings demonstrate that the Ser/Thr protein kinase PknB is essential for sustaining mycobacterial growth and support the development of protein kinase inhibitors as new potential antituberculosis drugs.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.