期刊
MOLECULAR CELL
卷 59, 期 2, 页码 309-320出版社
CELL PRESS
DOI: 10.1016/j.molcel.2015.06.013
关键词
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资金
- Australian National Health and Medical Research Council (NHMRC) [APP1023973]
- Australian Research Council
- Wellcome Trust
- European Research Council
- Cancer Research UK [22308] Funding Source: researchfish
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 monoADP- ribosylation. We propose that these posttranslational modifications modulate microbial virulence by regulating the response to host-derived reactive oxygen species.
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