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Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens

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Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens. / Rack, Johannes Gregor Matthias; Morra, Rosa; Barkauskaite, Eva et al.
In: Molecular Cell, Vol. 59, No. 2, 16.07.2015, p. 309-20.

Research output: Contribution to journal › Article › peer-review

HarvardHarvard

Rack, JGM, Morra, R, Barkauskaite, E, Kraehenbuehl, R, Ariza, A, Qu, Y, Ortmayer, M, Leidecker, O, Cameron, DR, Matic, I, Peleg, AY, Leys, D, Traven, A & Ahel, I 2015, 'Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens', Molecular Cell, vol. 59, no. 2, pp. 309-20. https://doi.org/10.1016/j.molcel.2015.06.013

APA

Rack, J. G. M., Morra, R., Barkauskaite, E., Kraehenbuehl, R., Ariza, A., Qu, Y., Ortmayer, M., Leidecker, O., Cameron, D. R., Matic, I., Peleg, A. Y., Leys, D., Traven, A., & Ahel, I. (2015). Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens. Molecular Cell, 59(2), 309-20. https://doi.org/10.1016/j.molcel.2015.06.013

CBE

Rack JGM, Morra R, Barkauskaite E, Kraehenbuehl R, Ariza A, Qu Y, Ortmayer M, Leidecker O, Cameron DR, Matic I, et al. 2015. Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens. Molecular Cell. 59(2):309-20. https://doi.org/10.1016/j.molcel.2015.06.013

MLA

Rack, Johannes Gregor Matthias et al. "Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens". Molecular Cell. 2015, 59(2). 309-20. https://doi.org/10.1016/j.molcel.2015.06.013

VancouverVancouver

Rack JGM, Morra R, Barkauskaite E, Kraehenbuehl R, Ariza A, Qu Y et al. Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens. Molecular Cell. 2015 Jul 16;59(2):309-20. Epub 2015 Jul 9. doi: 10.1016/j.molcel.2015.06.013

Author

Rack, Johannes Gregor Matthias ; Morra, Rosa ; Barkauskaite, Eva et al. / Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens. In: Molecular Cell. 2015 ; Vol. 59, No. 2. pp. 309-20.

RIS

TY - JOUR

T1 - Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens

AU - Rack, Johannes Gregor Matthias

AU - Morra, Rosa

AU - Barkauskaite, Eva

AU - Kraehenbuehl, Rolf

AU - Ariza, Antonio

AU - Qu, Yue

AU - Ortmayer, Mary

AU - Leidecker, Orsolya

AU - Cameron, David R

AU - Matic, Ivan

AU - Peleg, Anton Y

AU - Leys, David

AU - Traven, Ana

AU - Ahel, Ivan

N1 - Copyright © 2015 The Authors. Published by Elsevier Inc. All rights reserved.

PY - 2015/7/16

Y1 - 2015/7/16

N2 - Sirtuins are an ancient family of NAD(+)-dependent deacylases connected with the regulation of fundamental cellular processes including metabolic homeostasis and genome integrity. We show the existence of a hitherto unrecognized class of sirtuins, found predominantly in microbial pathogens. In contrast to earlier described classes, these sirtuins exhibit robust protein ADP-ribosylation activity. In our model organisms, Staphylococcus aureus and Streptococcus pyogenes, the activity is dependent on prior lipoylation of the target protein and can be reversed by a sirtuin-associated macrodomain protein. Together, our data describe a sirtuin-dependent reversible protein ADP-ribosylation system and establish a crosstalk between lipoylation and mono-ADP-ribosylation. We propose that these posttranslational modifications modulate microbial virulence by regulating the response to host-derived reactive oxygen species.

AB - Sirtuins are an ancient family of NAD(+)-dependent deacylases connected with the regulation of fundamental cellular processes including metabolic homeostasis and genome integrity. We show the existence of a hitherto unrecognized class of sirtuins, found predominantly in microbial pathogens. In contrast to earlier described classes, these sirtuins exhibit robust protein ADP-ribosylation activity. In our model organisms, Staphylococcus aureus and Streptococcus pyogenes, the activity is dependent on prior lipoylation of the target protein and can be reversed by a sirtuin-associated macrodomain protein. Together, our data describe a sirtuin-dependent reversible protein ADP-ribosylation system and establish a crosstalk between lipoylation and mono-ADP-ribosylation. We propose that these posttranslational modifications modulate microbial virulence by regulating the response to host-derived reactive oxygen species.

KW - Adenosine Diphosphate Ribose/metabolism

KW - Bacterial Proteins/chemistry

KW - Catalytic Domain

KW - Crystallography, X-Ray

KW - Genes, Bacterial

KW - HEK293 Cells

KW - Host-Pathogen Interactions

KW - Humans

KW - Lactobacillales/enzymology

KW - Lipoylation

KW - Models, Molecular

KW - Operon

KW - Oxidative Stress

KW - Phylogeny

KW - Protein Conformation

KW - Sirtuins/chemistry

KW - Staphylococcus aureus/enzymology

KW - Streptococcus pyogenes/enzymology

U2 - 10.1016/j.molcel.2015.06.013

DO - 10.1016/j.molcel.2015.06.013

M3 - Article

C2 - 26166706

VL - 59

SP - 309

EP - 320

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 2

ER -