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Monk, Ian R; Shaikh, Nausad; Begg, Stephanie L; Gajdiss, Mike; Sharkey, Liam K R; Lee, Jean Y H; Pidot, Sacha J; Seemann, Torsten; Kuiper, Michael; Winnen, Brit; Hvorup, Rikki; Collins, Brett M; Bierbaum, Gabriele; Udagedara, Saumya R; Morey, Jacqueline R; Pulyani, Neha; Howden, Benjamin P; Maher, Megan J; McDevitt, Christopher A; King, Glenn F; Stinear, Timothy P
Nature communications, 07/2019, Volume: 10, Issue: 1Journal Article
WalKR (YycFG) is the only essential two-component regulator in the human pathogen Staphylococcus aureus. WalKR regulates peptidoglycan synthesis, but this function alone does not explain its essentiality. Here, to further understand WalKR function, we investigate a suppressor mutant that arose when WalKR activity was impaired; a histidine to tyrosine substitution (H271Y) in the cytoplasmic Per-Arnt-Sim (PAS ) domain of the histidine kinase WalK. Introducing the WalK mutation into wild-type S. aureus activates the WalKR regulon. Structural analyses of the WalK PAS domain reveal a metal-binding site, in which a zinc ion (Zn ) is tetrahedrally-coordinated by four amino acids including H271. The WalK mutation abrogates metal binding, increasing WalK kinase activity and WalR phosphorylation. Thus, Zn -binding negatively regulates WalKR. Promoter-reporter experiments using S. aureus confirm Zn sensing by this system. Identification of a metal ligand recognized by the WalKR system broadens our understanding of this critical S. aureus regulon.
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