ArticleThe Journal of biological chemistry2009
The Mycobacterium tuberculosis protein kinase K modulates activation of transcription from the promoter of mycobacterial monooxygenase operon through phosphorylation of the transcriptional regulator VirS.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Protein-Mediated Virulence in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- The pathway of autophagy in the epigenetic landscape ofAutophagy · 2025Review
- Hit Compounds and Associated Targets in IntracellularMolecules (Basel, Switzerland) · 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
- Modulation of the M. tuberculosis cell envelope between replicating and non-replicating persistent bacteria.Tuberculosis (Edinburgh, Scotland) · 2020Review
- Mycobacterium tuberculosis serine/threonine protein kinases: structural information for the design of their specific ATP-competitive inhibitors.Journal of computer-aided molecular design · 2018Article
- Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments.International journal of molecular sciences · 2018Review
- Mycobacterium smegmatis PafBC is involved in regulation of DNA damage response.Scientific reports · 2017Article
- Epigenetic Phosphorylation Control of Mycobacterium tuberculosis Infection and Persistence.Microbiology spectrum · 2017Review
- Serine/Threonine Protein Phosphatase PstP of Mycobacterium tuberculosis Is Necessary for Accurate Cell Division and Survival of Pathogen.The Journal of biological chemistry · 2016Article
- RD-1 encoded EspJ protein gets phosphorylated prior to affect the growth and intracellular survival of mycobacteria.Scientific reports · 2015Article
- 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.The Journal of biological chemistry · 2015Article
- Article
- 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
- In silico prediction of protein-protein interactions in human macrophages.BMC research notes · 2014Article
- Regulation of transcription by eukaryotic-like serine-threonine kinases and phosphatases in Gram-positive bacterial pathogens.Virulence · 2014Review
- Development of a new generation of vectors for gene expression, gene replacement, and protein-protein interaction studies in mycobacteria.Applied and environmental microbiology · 2013Article
- Rv3080c regulates the rate of inhibition of mycobacteria by isoniazid through FabD.Molecular and cellular biochemistry · 2013Article
- Virulence factors of the Mycobacterium tuberculosis complex.Virulence · 2013Review
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7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycobacterium tuberculosis encodes for 11 eukaryotic-like serine/threonine protein kinases. Genetic and biochemical studies show that these kinases regulate various cellular processes including cell shape and morphology, glucose and glutamine transport, phagosome-lysosome fusion and the expression, and/or activity of transcription factors. PknK is the largest predicted serine/threonine protein kinase in M. tuberculosis. Here, we have cloned, overexpressed, and purified protein kinase K (PknK) to near homogeneity and show that its ability to phosphorylate proteins is dependent on the invariant lysine (Lys(55)), and on two conserved threonine residues present in its activation loop. Despite being devoid of any apparent transmembrane domain, PknK is localized to the cell wall fraction, suggesting probable anchoring of the kinase to the cell membrane region. The pknK gene is located in the vicinity of the virS gene, which is known to regulate the expression of the mycobacterial monooxygenase (mymA) operon. We report here for the first time that VirS is in fact a substrate of PknK. In addition, four of the proteins encoded by mymA operon are also found to be substrates of PknK. Results show that VirS is a bona fide substrate of PknK in vivo, and PknK-mediated phosphorylation of VirS increases its affinity for mym promoter DNA. Reporter assays reveal that PknK modulates VirS-mediated stimulation of transcription from the mym promoter. These findings suggest that the expression of mymA operon genes is regulated through PknK-mediated phosphorylation of VirS.
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