Data · dataset · 2026
Phosphorylation by the PknB Serine/Threonine Kinase Stimulates Dimer Formation by WalR
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WalKR is a two-component system that regulates cell wall homeostasis and other processes in low-GC Gram-positive bacteria.
Description
It is essential for viability in Staphylococcus aureus and regulates genes that encode the autolysins and other critical proteins. The sensor kinase WalK phosphorylates WalR at the aspartic acid residue 53 (D53) in the receiver domain, stimulating promoter DNA binding.
Unlike most response regulators, WalR is reported to have a second kinase, the serine/threonine kinase PknB, which phosphorylates the receiver domain at the threonine residue 101. We previously reported that a <i>walR</i> mutation that changed T101 to a methionine conferred low-level resistance to vancomycin and greatly increased susceptibility to tunicamycin along with several other phenotypic traits. In this work, we demonstrate similarities between <i>pknB</i> null and the WalR<sub>T101M</sub> mutants.
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A combination of <i>in vitro</i> and <i>in vivo</i> data supports the idea that PknB interacts with WalR in living cells (consistent with similar experiments in Bacillus subtilis) and that this likely involves phosphorylation of WalR at T101. Using <i>in silico</i> modeling, we identified a possible intermolecular hydrogen bond between the T101 phosphate group and E108. This would have the effect of stabilizing the WalR dimerization interface.
Consistent with this, we find that T101 is important for WalR dimer formation <i>in vivo</i>. The primary activation of WalR is clearly phosphorylation at D53 by WalK. However, our data suggest that PknB serves as a second potentiating input stabilizing the WalR dimer.
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Where it is published
- DOI doi.org/10.1021/acs.biochem.6c00334.s004 ↗
DOI / persistent id · from zivahub uct ac za
Catalogue records · 1
- OAI-PMH record api.figshare.com/v2/oai?verb=GetRecord&metadataPrefix=oai_dc&identifier=oai%3Af… ↗
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Topics
- From keywords
- Biochemistry and cell biology · Cancer · Earth & Environmental Science · Genetics · Immunology · Infectious diseases · Life Sciences · Medicine & Health · Microbiology
Related
- Possibly the same asPhosphorylation by the PknB Serine/Threonine Kinase Stimulates Dimer Formation by WalR
- Possibly the same asPhosphorylation by the PknB Serine/Threonine Kinase Stimulates Dimer Formation by WalR
- Possibly the same asPhosphorylation by the PknB Serine/Threonine Kinase Stimulates Dimer Formation by WalR
- Possibly the same asPhosphorylation by the PknB Serine/Threonine Kinase Stimulates Dimer Formation by WalR
Provenance · 1 source records, 14 field assertions
| Source | Key | Last seen | Raw |
|---|---|---|---|
| ZivaHub | oai:figshare.com:article/34027243 | 11 d ago | JSON v1 |
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| title | source · zivahub uct ac za | connector:zivahub_uct_ac_za@1.0.0 | /metadata/dc/title |