Zinc-binding to the cytoplasmic PAS domain regulates the essential WalK histidine kinase of Staphylococcus aureus

WalKR is an essential two-component regulator that controls peptidoglycan synthesis in the human pathogen Staphylococcus aureus. Here, the authors provide biochemical, structural, and functional evidence supporting that the binding of a zinc ion inhibits autophosphorylation and thus alters WalKR reg...

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Main Authors: Ian R. Monk, Nausad Shaikh, Stephanie L. Begg, Mike Gajdiss, Liam K. R. Sharkey, Jean Y. H. Lee, Sacha J. Pidot, Torsten Seemann, Michael Kuiper, Brit Winnen, Rikki Hvorup, Brett M. Collins, Gabriele Bierbaum, Saumya R. Udagedara, Jacqueline R. Morey, Neha Pulyani, Benjamin P. Howden, Megan J. Maher, Christopher A. McDevitt, Glenn F. King, Timothy P. Stinear
Format: Article
Language:English
Published: Nature Publishing Group 2019-07-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-10932-4
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spelling doaj-8c79c77e7e1c43c2b593eb5939e70c112021-05-11T12:15:59ZengNature Publishing GroupNature Communications2041-17232019-07-0110111310.1038/s41467-019-10932-4Zinc-binding to the cytoplasmic PAS domain regulates the essential WalK histidine kinase of Staphylococcus aureusIan R. Monk0Nausad Shaikh1Stephanie L. Begg2Mike Gajdiss3Liam K. R. Sharkey4Jean Y. H. Lee5Sacha J. Pidot6Torsten Seemann7Michael Kuiper8Brit WinnenRikki Hvorup9Brett M. Collins10Gabriele Bierbaum11Saumya R. Udagedara12Jacqueline R. Morey13Neha Pulyani14Benjamin P. Howden15Megan J. Maher16Christopher A. McDevitt17Glenn F. King18Timothy P. Stinear19Department of Microbiology and Immunology, Doherty Institute for Infection and Immunity, University of MelbourneInstitute for Molecular Bioscience, The University of QueenslandDepartment of Microbiology and Immunology, Doherty Institute for Infection and Immunity, University of MelbourneUniversity Clinics of Bonn, Institute of Medical Microbiology, Immunology and ParasitologyDepartment of Microbiology and Immunology, Doherty Institute for Infection and Immunity, University of MelbourneDepartment of Microbiology and Immunology, Doherty Institute for Infection and Immunity, University of MelbourneDepartment of Microbiology and Immunology, Doherty Institute for Infection and Immunity, University of MelbourneDepartment of Microbiology and Immunology, Doherty Institute for Infection and Immunity, University of MelbourneCSIRO Data61Institute for Molecular Bioscience, The University of QueenslandInstitute for Molecular Bioscience, The University of QueenslandUniversity Clinics of Bonn, Institute of Medical Microbiology, Immunology and ParasitologyDepartment of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe UniversityDepartment of Molecular and Biomedical Sciences, School of Biological Sciences, The University of AdelaideDepartment of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe UniversityDepartment of Microbiology and Immunology, Doherty Institute for Infection and Immunity, University of MelbourneDepartment of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe UniversityDepartment of Microbiology and Immunology, Doherty Institute for Infection and Immunity, University of MelbourneInstitute for Molecular Bioscience, The University of QueenslandDepartment of Microbiology and Immunology, Doherty Institute for Infection and Immunity, University of MelbourneWalKR is an essential two-component regulator that controls peptidoglycan synthesis in the human pathogen Staphylococcus aureus. Here, the authors provide biochemical, structural, and functional evidence supporting that the binding of a zinc ion inhibits autophosphorylation and thus alters WalKR regulatory activity.https://doi.org/10.1038/s41467-019-10932-4
collection DOAJ
language English
format Article
sources DOAJ
author Ian R. Monk
Nausad Shaikh
Stephanie L. Begg
Mike Gajdiss
Liam K. R. Sharkey
Jean Y. H. Lee
Sacha J. Pidot
Torsten Seemann
Michael Kuiper
Brit Winnen
Rikki Hvorup
Brett M. Collins
Gabriele Bierbaum
Saumya R. Udagedara
Jacqueline R. Morey
Neha Pulyani
Benjamin P. Howden
Megan J. Maher
Christopher A. McDevitt
Glenn F. King
Timothy P. Stinear
spellingShingle Ian R. Monk
Nausad Shaikh
Stephanie L. Begg
Mike Gajdiss
Liam K. R. Sharkey
Jean Y. H. Lee
Sacha J. Pidot
Torsten Seemann
Michael Kuiper
Brit Winnen
Rikki Hvorup
Brett M. Collins
Gabriele Bierbaum
Saumya R. Udagedara
Jacqueline R. Morey
Neha Pulyani
Benjamin P. Howden
Megan J. Maher
Christopher A. McDevitt
Glenn F. King
Timothy P. Stinear
Zinc-binding to the cytoplasmic PAS domain regulates the essential WalK histidine kinase of Staphylococcus aureus
Nature Communications
author_facet Ian R. Monk
Nausad Shaikh
Stephanie L. Begg
Mike Gajdiss
Liam K. R. Sharkey
Jean Y. H. Lee
Sacha J. Pidot
Torsten Seemann
Michael Kuiper
Brit Winnen
Rikki Hvorup
Brett M. Collins
Gabriele Bierbaum
Saumya R. Udagedara
Jacqueline R. Morey
Neha Pulyani
Benjamin P. Howden
Megan J. Maher
Christopher A. McDevitt
Glenn F. King
Timothy P. Stinear
author_sort Ian R. Monk
title Zinc-binding to the cytoplasmic PAS domain regulates the essential WalK histidine kinase of Staphylococcus aureus
title_short Zinc-binding to the cytoplasmic PAS domain regulates the essential WalK histidine kinase of Staphylococcus aureus
title_full Zinc-binding to the cytoplasmic PAS domain regulates the essential WalK histidine kinase of Staphylococcus aureus
title_fullStr Zinc-binding to the cytoplasmic PAS domain regulates the essential WalK histidine kinase of Staphylococcus aureus
title_full_unstemmed Zinc-binding to the cytoplasmic PAS domain regulates the essential WalK histidine kinase of Staphylococcus aureus
title_sort zinc-binding to the cytoplasmic pas domain regulates the essential walk histidine kinase of staphylococcus aureus
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2019-07-01
description WalKR is an essential two-component regulator that controls peptidoglycan synthesis in the human pathogen Staphylococcus aureus. Here, the authors provide biochemical, structural, and functional evidence supporting that the binding of a zinc ion inhibits autophosphorylation and thus alters WalKR regulatory activity.
url https://doi.org/10.1038/s41467-019-10932-4
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