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The DNA-binding induced (de)AMPylation activity of a Coxiella burnetii Fic enzyme targets Histone H3

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The DNA-binding induced (de)AMPylation activity of a Coxiella burnetii Fic enzyme targets Histone H3. / Höpfner, Dorothea; Cichy, Adam; Pogenberg, Vivian; Krisp, Christoph; Mezouar, Soraya; Bach, Nina C; Grotheer, Jan; Zarza, Sandra Madariaga; Martinez, Eric; Bonazzi, Matteo; Feige, Matthias J; Sieber, Stephan A; Schlüter, Hartmut; Itzen, Aymelt.

in: COMMUN BIOL, Jahrgang 6, Nr. 1, 06.11.2023, S. 1124.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Höpfner, D, Cichy, A, Pogenberg, V, Krisp, C, Mezouar, S, Bach, NC, Grotheer, J, Zarza, SM, Martinez, E, Bonazzi, M, Feige, MJ, Sieber, SA, Schlüter, H & Itzen, A 2023, 'The DNA-binding induced (de)AMPylation activity of a Coxiella burnetii Fic enzyme targets Histone H3', COMMUN BIOL, Jg. 6, Nr. 1, S. 1124. https://doi.org/10.1038/s42003-023-05494-7

APA

Höpfner, D., Cichy, A., Pogenberg, V., Krisp, C., Mezouar, S., Bach, N. C., Grotheer, J., Zarza, S. M., Martinez, E., Bonazzi, M., Feige, M. J., Sieber, S. A., Schlüter, H., & Itzen, A. (2023). The DNA-binding induced (de)AMPylation activity of a Coxiella burnetii Fic enzyme targets Histone H3. COMMUN BIOL, 6(1), 1124. https://doi.org/10.1038/s42003-023-05494-7

Vancouver

Höpfner D, Cichy A, Pogenberg V, Krisp C, Mezouar S, Bach NC et al. The DNA-binding induced (de)AMPylation activity of a Coxiella burnetii Fic enzyme targets Histone H3. COMMUN BIOL. 2023 Nov 6;6(1):1124. https://doi.org/10.1038/s42003-023-05494-7

Bibtex

@article{08c5e55ef0ab418b86267f00c99e3ce6,
title = "The DNA-binding induced (de)AMPylation activity of a Coxiella burnetii Fic enzyme targets Histone H3",
abstract = "The intracellular bacterial pathogen Coxiella burnetii evades the host response by secreting effector proteins that aid in establishing a replication-friendly niche. Bacterial filamentation induced by cyclic AMP (Fic) enzymes can act as effectors by covalently modifying target proteins with the posttranslational AMPylation by transferring adenosine monophosphate (AMP) from adenosine triphosphate (ATP) to a hydroxyl-containing side chain. Here we identify the gene product of C. burnetii CBU_0822, termed C. burnetii Fic 2 (CbFic2), to AMPylate host cell histone H3 at serine 10 and serine 28. We show that CbFic2 acts as a bifunctional enzyme, both capable of AMPylation as well as deAMPylation, and is regulated by the binding of DNA via a C-terminal helix-turn-helix domain. We propose that CbFic2 performs AMPylation in its monomeric state, switching to a deAMPylating dimer upon DNA binding. This study unveils reversible histone modification by a specific enzyme of a pathogenic bacterium.",
keywords = "Cyclic AMP, Histones, Coxiella burnetii, DNA, Serine",
author = "Dorothea H{\"o}pfner and Adam Cichy and Vivian Pogenberg and Christoph Krisp and Soraya Mezouar and Bach, {Nina C} and Jan Grotheer and Zarza, {Sandra Madariaga} and Eric Martinez and Matteo Bonazzi and Feige, {Matthias J} and Sieber, {Stephan A} and Hartmut Schl{\"u}ter and Aymelt Itzen",
note = "{\textcopyright} 2023. The Author(s).",
year = "2023",
month = nov,
day = "6",
doi = "10.1038/s42003-023-05494-7",
language = "English",
volume = "6",
pages = "1124",
journal = "COMMUN BIOL",
issn = "2399-3642",
publisher = "NATURE PUBLISHING GROUP",
number = "1",

}

RIS

TY - JOUR

T1 - The DNA-binding induced (de)AMPylation activity of a Coxiella burnetii Fic enzyme targets Histone H3

AU - Höpfner, Dorothea

AU - Cichy, Adam

AU - Pogenberg, Vivian

AU - Krisp, Christoph

AU - Mezouar, Soraya

AU - Bach, Nina C

AU - Grotheer, Jan

AU - Zarza, Sandra Madariaga

AU - Martinez, Eric

AU - Bonazzi, Matteo

AU - Feige, Matthias J

AU - Sieber, Stephan A

AU - Schlüter, Hartmut

AU - Itzen, Aymelt

N1 - © 2023. The Author(s).

PY - 2023/11/6

Y1 - 2023/11/6

N2 - The intracellular bacterial pathogen Coxiella burnetii evades the host response by secreting effector proteins that aid in establishing a replication-friendly niche. Bacterial filamentation induced by cyclic AMP (Fic) enzymes can act as effectors by covalently modifying target proteins with the posttranslational AMPylation by transferring adenosine monophosphate (AMP) from adenosine triphosphate (ATP) to a hydroxyl-containing side chain. Here we identify the gene product of C. burnetii CBU_0822, termed C. burnetii Fic 2 (CbFic2), to AMPylate host cell histone H3 at serine 10 and serine 28. We show that CbFic2 acts as a bifunctional enzyme, both capable of AMPylation as well as deAMPylation, and is regulated by the binding of DNA via a C-terminal helix-turn-helix domain. We propose that CbFic2 performs AMPylation in its monomeric state, switching to a deAMPylating dimer upon DNA binding. This study unveils reversible histone modification by a specific enzyme of a pathogenic bacterium.

AB - The intracellular bacterial pathogen Coxiella burnetii evades the host response by secreting effector proteins that aid in establishing a replication-friendly niche. Bacterial filamentation induced by cyclic AMP (Fic) enzymes can act as effectors by covalently modifying target proteins with the posttranslational AMPylation by transferring adenosine monophosphate (AMP) from adenosine triphosphate (ATP) to a hydroxyl-containing side chain. Here we identify the gene product of C. burnetii CBU_0822, termed C. burnetii Fic 2 (CbFic2), to AMPylate host cell histone H3 at serine 10 and serine 28. We show that CbFic2 acts as a bifunctional enzyme, both capable of AMPylation as well as deAMPylation, and is regulated by the binding of DNA via a C-terminal helix-turn-helix domain. We propose that CbFic2 performs AMPylation in its monomeric state, switching to a deAMPylating dimer upon DNA binding. This study unveils reversible histone modification by a specific enzyme of a pathogenic bacterium.

KW - Cyclic AMP

KW - Histones

KW - Coxiella burnetii

KW - DNA

KW - Serine

U2 - 10.1038/s42003-023-05494-7

DO - 10.1038/s42003-023-05494-7

M3 - SCORING: Journal article

C2 - 37932372

VL - 6

SP - 1124

JO - COMMUN BIOL

JF - COMMUN BIOL

SN - 2399-3642

IS - 1

ER -