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Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography I04-1-Macromolecular Crystallography (fixed wavelength)	Identification of a class of protein ADP-ribosylating sirtuins in microbial pathogens Johannes Gregor Matthias Rack , Rosa Morra , Eva Barkauskaite , Rolf Kraehenbuehl , Antonio Ariza , Yue Qu , Mary Ortmayer , Orsolya Leidecker , David r Cameron , Ivan Matic , Anton y. Peleg , David Leys , Ana Traven , Ivan Ahel Molecular Cell 59 (2), 309–320 DOI: 10.1016/j.molcel.2015.06.013 PMID: 26166706 Diamond Proposal Number(s): [9306] Open Access Show Abstract ▼ 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.	Jul 2015

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