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Table · dataset · 2026

Phosphorylation by the PknB Serine/Threonine Kinase Stimulates Dimer Formation by WalR

Listed in ZivaHub and HKU DataHub and DaYta Ya Rona and figshare and Loughborough Research Repository and UP Research Data Repository — shown once because both records carry DOI 10.1021/acs.biochem.6c00334.s005

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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Provenance · 6 source records, 82 field assertions
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ZivaHuboai:figshare.com:article/3402724611 d agoJSON v1
HKU DataHuboai:figshare.com:article/3402724611 d agoJSON v1
DaYta Ya Ronaoai:figshare.com:article/3402724611 d agoJSON v1
figshareoai:figshare.com:article/3402724610 d agoJSON v1
Loughborough Research Repositoryoai:figshare.com:article/3402724610 d agoJSON v1
UP Research Data Repositoryoai:figshare.com:article/3402724610 d agoJSON v1
FieldAssertionExtractorEvidence
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