ArticlePloS one2010
Understanding the role of PknJ in Mycobacterium tuberculosis: biochemical characterization and identification of novel substrate pyruvate kinase A.
Article in PloS one, 2010. 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, 53 citations in OpenAlex.
- Export of eDNA is a mechanism used by Mycobacterium avium subsp. hominissuis for survival within host macrophages.Archives of microbiology · 2025Article
- Giving a signal: how protein phosphorylation helps Bacillus navigate through different life stages.FEMS microbiology reviews · 2023Review
- Stringent Response in Mycobacteria: From Biology to Therapeutic Potential.Pathogens (Basel, Switzerland) · 2021Review
- Artificial Intelligence in Surveillance, Diagnosis, Drug Discovery and Vaccine Development against COVID-19.Pathogens (Basel, Switzerland) · 2021Review
- Phosphoproteome Study ofFrontiers in microbiology · 2021Article
- NU-6027 Inhibits Growth of Mycobacterium tuberculosis by Targeting Protein Kinase D and Protein Kinase G.Antimicrobial agents and chemotherapy · 2019Article
- The Ser/Thr protein kinase PrkC imprints phenotypic memory inThe Journal of biological chemistry · 2019Article
- Investigation of the phosphorylation of Bacillus subtilis LTA synthases by the serine/threonine kinase PrkC.Scientific reports · 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
- Epigenetic Phosphorylation Control of Mycobacterium tuberculosis Infection and Persistence.Microbiology spectrum · 2017Review
- The Eukaryote-Like Serine/Threonine Kinase STK Regulates the Growth and Metabolism of ZoonoticFrontiers in cellular and infection microbiology · 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
- 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
- Protein synthesis during cellular quiescence is inhibited by phosphorylation of a translational elongation factor.Proceedings of the National Academy of Sciences of the United States of America · 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
- Phosphoproteomics analysis of a clinical Mycobacterium tuberculosis Beijing isolate: expanding the mycobacterial phosphoproteome catalog.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
- Article
- Rv3080c regulates the rate of inhibition of mycobacteria by isoniazid through FabD.Molecular and cellular biochemistry · 2013Article
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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
Reversible protein phosphorylation is a prevalent signaling mechanism which modulates cellular metabolism in response to changing environmental conditions. In this study, we focus on previously uncharacterized Mycobacterium tuberculosis Ser/Thr protein kinase (STPK) PknJ, a putative transmembrane protein. PknJ is shown to possess autophosphorylation activity and is also found to be capable of carrying out phosphorylation on the artificial substrate myelin basic protein (MyBP). Previous studies have shown that the autophosphorylation activity of M. tuberculosis STPKs is dependent on the conserved residues in the activation loop. However, our results show that apart from the conventional conserved residues, additional residues in the activation loop may also play a crucial role in kinase activation. Further characterization of PknJ reveals that the kinase utilizes unusual ions (Ni(2+), Co(2+)) as cofactors, thus hinting at a novel mechanism for PknJ activation. Additionally, as shown for other STPKs, we observe that PknJ possesses the capability to dimerize. In order to elucidate the signal transduction cascade emanating from PknJ, the M. tuberculosis membrane-associated protein fraction is treated with the active kinase and glycolytic enzyme Pyruvate kinase A (mtPykA) is identified as one of the potential substrates of PknJ. The phospholabel is found to be localized on serine and threonine residue(s), with Ser(37) identified as one of the sites of phosphorylation. Since Pyk is known to catalyze the last step of glycolysis, our study shows that the fundamental pathways such as glycolysis can also be governed by STPK-mediated signaling.
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