ArticleNature communications2019
LipidII interaction with specific residues of Mycobacterium tuberculosis PknB extracytoplasmic domain governs its optimal activation.
Article in Nature communications, 2019. 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, 58 citations in OpenAlex.
- A lipid cue drives the subcellular localization of a self-inserting bacterial transmembrane protein.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Polar growth factor PgfA regulates polar peptidoglycan synthesis as well as mycolate synthesis inJournal of bacteriology · 2026Article
- Structural dissection of the catalytic domain of the serine threonine kinase StkP of Streptococcus pneumoniae.Nature communications · 2026Article
- Influence of SmpB and ClpX interactions and interactomes on the transcription profile of Mycobacterium tuberculosis.The Biochemical journal · 2026Article
- A lipid cue drives the subcellular localization of a self-inserting bacterial transmembrane protein.bioRxiv : the preprint server for biology · 2026Article
- A Hanks-type bacterial kinase, PknS, directly phosphorylates the alternative sigma factor EcfK to promote resistance to protist predation.The FEBS journal · 2026Article
- Effects of CwlM, a peptidoglycan synthesis regulator, on beta-lactam tolerance and host-pathogen interactions.BMC microbiology · 2025Article
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- An atlas of bacterial serine-threonine kinases reveals functional diversity and key distinctions from eukaryotic kinases.Science signaling · 2025Article
- GpsB Coordinates StkP Signaling as a PASTA Kinase Adaptor in Streptococcus pneumoniae Cell Division.Journal of molecular biology · 2024Article
- Negative regulation of MurZ and MurA underlies the essentiality of GpsB- and StkP-mediated protein phosphorylation in Streptococcus pneumoniae D39.Molecular microbiology · 2023Article
- Giving a signal: how protein phosphorylation helps Bacillus navigate through different life stages.FEMS microbiology reviews · 2023Review
- A multiomic approach to defining the essential genome of the globally important pathogen Corynebacterium diphtheriae.PLoS genetics · 2023Article
- Growth rate is modulated by monitoring cell wall precursors in Bacillus subtilis.Nature microbiology · 2023Article
- Amidation of glutamate residues in mycobacterial peptidoglycan is essential for cell wall cross-linking.Frontiers in cellular and infection microbiology · 2023Article
- SigE: A master regulator ofFrontiers in microbiology · 2023Review
- Article
- MiaA (Rv2727c) mediated tRNA isopentenylation ofMolecular biology research communications · 2022Article
- Crosstalk between guanosine nucleotides regulates cellular heterogeneity in protein synthesis during nutrient limitation.PLoS genetics · 2022Article
- MurA escape mutations uncouple peptidoglycan biosynthesis from PrkA signaling.PLoS pathogens · 2022Article
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Authors and funding
14 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Mycobacterium tuberculosis kinase PknB is essential for growth and survival of the pathogen in vitro and in vivo. Here we report the results of our efforts to elucidate the mechanism of regulation of PknB activity. The specific residues in the PknB extracytoplasmic domain that are essential for ligand interaction and survival of the bacterium are identified. The extracytoplasmic domain interacts with mDAP-containing LipidII, and this is abolished upon mutation of the ligand-interacting residues. Abrogation of ligand-binding or sequestration of the ligand leads to aberrant localization of PknB. Contrary to the prevailing hypothesis, abrogation of ligand-binding is linked to activation loop hyperphosphorylation, and indiscriminate hyperphosphorylation of PknB substrates as well as other proteins, ultimately causing loss of homeostasis and cell death. We propose that the ligand-kinase interaction directs the appropriate localization of the kinase, coupled to stringently controlled activation of PknB, and consequently the downstream processes thereof.
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