Abstract
Nε-acetylation is emerging as an abundant post-translational modification of bacterial proteins. Two mechanisms have been identified: one is enzymatic, dependent on an acetyltransferase and acetyl-coenzyme A; the other is non-enzymatic and depends on the reactivity of acetyl phosphate. Some, but not most, of those acetylations are reversed by deacetylases. This review will briefly describe the current status of the field and raise questions that need answering.
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Acknowledgments
This work was supported by grants from the NIGMS (R01 GM066130) and the DOE (DE-SC00124430. I would like to acknowledge my collaborators, Bradford Gibson, Wayne Anderson and Christopher Rao, as well as present and former members of my laboratory.
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Communicated by M. Kupiec.
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Wolfe, A.J. Bacterial protein acetylation: new discoveries unanswered questions. Curr Genet 62, 335–341 (2016). https://doi.org/10.1007/s00294-015-0552-4
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DOI: https://doi.org/10.1007/s00294-015-0552-4