Rack, J.G.M., Morra, R., Barkauskaite, E. et al. (11 more authors) (2015) Identification of a class of protein ADP-ribosylating sirtuins in microbial pathogens. Molecular Cell, 59 (2). pp. 309-320. ISSN 1097-2765
Abstract
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2015 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
Keywords: | Adenosine Diphosphate Ribose; Bacterial Proteins; Catalytic Domain; Crystallography, X-Ray; Genes, Bacterial; HEK293 Cells; Host-Pathogen Interactions; Humans; Lactobacillales; Lipoylation; Models, Molecular; Operon; Oxidative Stress; Phylogeny; Protein Conformation; Sirtuins; Staphylococcus aureus; Streptococcus pyogenes |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 05 Jul 2023 13:00 |
Last Modified: | 05 Jul 2023 13:00 |
Status: | Published |
Publisher: | Elsevier BV |
Refereed: | Yes |
Identification Number: | 10.1016/j.molcel.2015.06.013 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:201221 |