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Binding of Cyclic Di-AMP to the Staphylococcus aureus Sensor Kinase KdpD Occurs via the Universal Stress Protein Domain and Downregulates the Expression of the Kdp Potassium Transporter

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Standard

Binding of Cyclic Di-AMP to the Staphylococcus aureus Sensor Kinase KdpD Occurs via the Universal Stress Protein Domain and Downregulates the Expression of the Kdp Potassium Transporter. / Moscoso, Joana A.; Schramke, Hannah; Zhang, Yong; Tosi, Tommaso; Dehbi, Amina; Jung, Kirsten; Gründling, Angelika.

I: Journal of Bacteriology, Bind 198, Nr. 1, 2016, s. 98-110.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Moscoso, JA, Schramke, H, Zhang, Y, Tosi, T, Dehbi, A, Jung, K & Gründling, A 2016, 'Binding of Cyclic Di-AMP to the Staphylococcus aureus Sensor Kinase KdpD Occurs via the Universal Stress Protein Domain and Downregulates the Expression of the Kdp Potassium Transporter', Journal of Bacteriology, bind 198, nr. 1, s. 98-110. https://doi.org/10.1128/JB.00480-15

APA

Moscoso, J. A., Schramke, H., Zhang, Y., Tosi, T., Dehbi, A., Jung, K., & Gründling, A. (2016). Binding of Cyclic Di-AMP to the Staphylococcus aureus Sensor Kinase KdpD Occurs via the Universal Stress Protein Domain and Downregulates the Expression of the Kdp Potassium Transporter. Journal of Bacteriology, 198(1), 98-110. https://doi.org/10.1128/JB.00480-15

Vancouver

Moscoso JA, Schramke H, Zhang Y, Tosi T, Dehbi A, Jung K o.a. Binding of Cyclic Di-AMP to the Staphylococcus aureus Sensor Kinase KdpD Occurs via the Universal Stress Protein Domain and Downregulates the Expression of the Kdp Potassium Transporter. Journal of Bacteriology. 2016;198(1):98-110. https://doi.org/10.1128/JB.00480-15

Author

Moscoso, Joana A. ; Schramke, Hannah ; Zhang, Yong ; Tosi, Tommaso ; Dehbi, Amina ; Jung, Kirsten ; Gründling, Angelika. / Binding of Cyclic Di-AMP to the Staphylococcus aureus Sensor Kinase KdpD Occurs via the Universal Stress Protein Domain and Downregulates the Expression of the Kdp Potassium Transporter. I: Journal of Bacteriology. 2016 ; Bind 198, Nr. 1. s. 98-110.

Bibtex

@article{0842cc4e3b2648469a86aed589f84900,
title = "Binding of Cyclic Di-AMP to the Staphylococcus aureus Sensor Kinase KdpD Occurs via the Universal Stress Protein Domain and Downregulates the Expression of the Kdp Potassium Transporter",
abstract = "Nucleotide signaling molecules are important intracellular messengers that regulate a wide range of biological functions. The human pathogen Staphylococcus aureus produces the signaling nucleotide cyclic di-AMP (c-di-AMP). This molecule is common among Gram-positive bacteria and in many organisms is essential for survival under standard laboratory growth conditions. In this study, we investigated the interaction of c-di-AMP with the S. aureus KdpD protein. The sensor kinase KdpD forms a two-component signaling system with the response regulator KdpE and regulates the expression of the kdpDE genes and the kdp-FABC operon coding for the Kdp potassium transporter components. Here we show that the S. aureus KdpD protein binds c-di-AMP specifically and with an affinity in the micromolar range through its universal stress protein (USP) domain. This domain is located within the N-terminal cytoplasmic region of KdpD, and amino acids of a conserved SXS-X20-FTAXY motif are important for this binding. We further show that KdpD2, a second KdpD protein found in some S. aureus strains, also binds c-di-AMP, and our bioinformatics analysis indicates that a subclass of KdpD proteins in c-di-AMP-producing bacteria has evolved to bind this signaling nucleotide. Finally, we show that c-di-AMP binding to KdpD inhibits the upregulation of the kdpFABC operon under salt stress, thus indicating that c-di-AMP is a negative regulator of potassium uptake in S. aureus.",
author = "Moscoso, {Joana A.} and Hannah Schramke and Yong Zhang and Tommaso Tosi and Amina Dehbi and Kirsten Jung and Angelika Gr{\"u}ndling",
year = "2016",
doi = "10.1128/JB.00480-15",
language = "English",
volume = "198",
pages = "98--110",
journal = "Journal of Bacteriology",
issn = "0021-9193",
publisher = "American Society for Microbiology",
number = "1",

}

RIS

TY - JOUR

T1 - Binding of Cyclic Di-AMP to the Staphylococcus aureus Sensor Kinase KdpD Occurs via the Universal Stress Protein Domain and Downregulates the Expression of the Kdp Potassium Transporter

AU - Moscoso, Joana A.

AU - Schramke, Hannah

AU - Zhang, Yong

AU - Tosi, Tommaso

AU - Dehbi, Amina

AU - Jung, Kirsten

AU - Gründling, Angelika

PY - 2016

Y1 - 2016

N2 - Nucleotide signaling molecules are important intracellular messengers that regulate a wide range of biological functions. The human pathogen Staphylococcus aureus produces the signaling nucleotide cyclic di-AMP (c-di-AMP). This molecule is common among Gram-positive bacteria and in many organisms is essential for survival under standard laboratory growth conditions. In this study, we investigated the interaction of c-di-AMP with the S. aureus KdpD protein. The sensor kinase KdpD forms a two-component signaling system with the response regulator KdpE and regulates the expression of the kdpDE genes and the kdp-FABC operon coding for the Kdp potassium transporter components. Here we show that the S. aureus KdpD protein binds c-di-AMP specifically and with an affinity in the micromolar range through its universal stress protein (USP) domain. This domain is located within the N-terminal cytoplasmic region of KdpD, and amino acids of a conserved SXS-X20-FTAXY motif are important for this binding. We further show that KdpD2, a second KdpD protein found in some S. aureus strains, also binds c-di-AMP, and our bioinformatics analysis indicates that a subclass of KdpD proteins in c-di-AMP-producing bacteria has evolved to bind this signaling nucleotide. Finally, we show that c-di-AMP binding to KdpD inhibits the upregulation of the kdpFABC operon under salt stress, thus indicating that c-di-AMP is a negative regulator of potassium uptake in S. aureus.

AB - Nucleotide signaling molecules are important intracellular messengers that regulate a wide range of biological functions. The human pathogen Staphylococcus aureus produces the signaling nucleotide cyclic di-AMP (c-di-AMP). This molecule is common among Gram-positive bacteria and in many organisms is essential for survival under standard laboratory growth conditions. In this study, we investigated the interaction of c-di-AMP with the S. aureus KdpD protein. The sensor kinase KdpD forms a two-component signaling system with the response regulator KdpE and regulates the expression of the kdpDE genes and the kdp-FABC operon coding for the Kdp potassium transporter components. Here we show that the S. aureus KdpD protein binds c-di-AMP specifically and with an affinity in the micromolar range through its universal stress protein (USP) domain. This domain is located within the N-terminal cytoplasmic region of KdpD, and amino acids of a conserved SXS-X20-FTAXY motif are important for this binding. We further show that KdpD2, a second KdpD protein found in some S. aureus strains, also binds c-di-AMP, and our bioinformatics analysis indicates that a subclass of KdpD proteins in c-di-AMP-producing bacteria has evolved to bind this signaling nucleotide. Finally, we show that c-di-AMP binding to KdpD inhibits the upregulation of the kdpFABC operon under salt stress, thus indicating that c-di-AMP is a negative regulator of potassium uptake in S. aureus.

U2 - 10.1128/JB.00480-15

DO - 10.1128/JB.00480-15

M3 - Journal article

C2 - 26195599

AN - SCOPUS:84953897479

VL - 198

SP - 98

EP - 110

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 1

ER -

ID: 227660989