ArticleThe Journal of biological chemistry2015
Protein kinase A (PknA) of Mycobacterium tuberculosis is independently activated and is critical for growth in vitro and survival of the pathogen in the host.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 50 citations in OpenAlex.
- Structural insights into multitargetingMicrobiology spectrum · 2026Article
- Structural and mechanistic basis of ubiquitous bacterial kinase signaling identifies PorX as a noncanonical substrate in Porphyromonas gingivalis.The Journal of biological chemistry · 2026Article
- Structural Modification of Indole Derivatives as PknB Inhibitors for Enhanced Enzymatic Inhibition and Antimycobacterial Activity.ACS omega · 2026Article
- Unravelling the protective effects: PknJ modulates MmaA4 expression and rifampicin susceptibility in Mycobacterium bovis BCG.Archives of microbiology · 2026Article
- Article
- An atlas of bacterial serine-threonine kinases reveals functional diversity and key distinctions from eukaryotic kinases.Science signaling · 2025Article
- Age-Dependent Pleomorphism inMicroorganisms · 2025Article
- Spatial segregation and aging of metabolic processes underlie phenotypic heterogeneity in mycobacteria.bioRxiv : the preprint server for biology · 2023Article
- Comprehensive essentiality analysis of themBio · 2023Article
- Mycobacterial Genetic Technologies for Probing the Host-Pathogen Microenvironment.Infection and immunity · 2023Review
- PeSTK db a comprehensive data repository of Probiotic Serine Threonine kinases.Scientific data · 2022Article
- Bacterial Protein Kinases.Advances in experimental medicine and biology · 2021Article
- Article
- Probing the Highly Disparate Dual Inhibitory Mechanisms of Novel Quinazoline Derivatives againstMolecules (Basel, Switzerland) · 2020Article
- Protein kinases PknA and PknB independently and coordinately regulate essential Mycobacterium tuberculosis physiologies and antimicrobial susceptibility.PLoS pathogens · 2020Article
- Phosphoproteomic Approaches to Discover Novel Substrates of Mycobacterial Ser/Thr Protein Kinases.Molecular & cellular proteomics : MCP · 2020Review
- Malaria and tuberculosis as diseases of neglected populations: state of the art in chemotherapy and advances in the search for new drugs.Memorias do Instituto Oswaldo Cruz · 2020Review
- NU-6027 Inhibits Growth of Mycobacterium tuberculosis by Targeting Protein Kinase D and Protein Kinase G.Antimicrobial agents and chemotherapy · 2019Article
- Novel mechanistic insights into physiological signaling pathways mediated by mycobacterial Ser/Thr protein kinases.Genes and immunity · 2019Review
- LipidII interaction with specific residues of Mycobacterium tuberculosis PknB extracytoplasmic domain governs its optimal activation.Nature communications · 2019Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The essential mycobacterial protein kinases PknA and PknB play crucial roles in modulating cell shape and division. However, the precise in vivo functional aspects of PknA have not been investigated. This study aims to dissect the role of PknA in mediating cell survival in vitro as well as in vivo. We observed aberrant cell shape and severe growth defects when PknA was depleted. Using the mouse infection model, we observe that PknA is essential for survival of the pathogen in the host. Complementation studies affirm the importance of the kinase, juxtamembrane, and transmembrane domains of PknA. Surprisingly, the extracytoplasmic domain is dispensable for cell growth and survival in vitro. We find that phosphorylation of the activation loop at Thr(172) of PknA is critical for bacterial growth. PknB has been previously suggested to be the receptor kinase, which activates multiple kinases, including PknA, by trans-phosphorylating their activation loop residues. Using phospho-specific PknA antibodies and conditional pknB mutant, we find that PknA autophosphorylates its activation loop independent of PknB. Fluorescently tagged PknA and PknB show distinctive distribution patterns within the cell, suggesting that although both kinases are known to modulate cell shape and division, their modes of action are likely to be different. This is supported by our findings that expression of kinase-dead PknA versus kinase-dead PknB in mycobacterial cells leads to different cellular phenotypes. Data indicate that although PknA and PknB are expressed as part of the same operon, they appear to be regulating cellular processes through divergent signaling pathways.
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