2014
DOI: 10.1371/journal.pone.0094816
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Structural, Kinetic and Proteomic Characterization of Acetyl Phosphate-Dependent Bacterial Protein Acetylation

Abstract: The emerging view of Nε-lysine acetylation in eukaryotes is of a relatively abundant post-translational modification (PTM) that has a major impact on the function, structure, stability and/or location of thousands of proteins involved in diverse cellular processes. This PTM is typically considered to arise by the donation of the acetyl group from acetyl-coenzyme A (acCoA) to the ε-amino group of a lysine residue that is reversibly catalyzed by lysine acetyltransferases and deacetylases. Here, we provide geneti… Show more

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Cited by 242 publications
(558 citation statements)
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References 95 publications
(139 reference statements)
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“…Although these experiments clearly indicate that cross-talk exists between the modifications, we cannot rule out the possibility that the acetyl phosphate used as the phospho-donor was also able to acetylate RprY. In fact, it was reported that in E. coli there is a second non-enzymatic mechanism with acetyl phosphate generated from glycolysis [22,30]. Although beyond the scope of the present study, future experiments will be carried out to determine whether acetyl phosphate can also acetylate RprY.…”
Section: Discussionmentioning
confidence: 88%
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“…Although these experiments clearly indicate that cross-talk exists between the modifications, we cannot rule out the possibility that the acetyl phosphate used as the phospho-donor was also able to acetylate RprY. In fact, it was reported that in E. coli there is a second non-enzymatic mechanism with acetyl phosphate generated from glycolysis [22,30]. Although beyond the scope of the present study, future experiments will be carried out to determine whether acetyl phosphate can also acetylate RprY.…”
Section: Discussionmentioning
confidence: 88%
“…These data indicated that RprY was acetylated in vivo with the involvement of Pat activity. Several studies showed that proteins can be chemically acetylated with either acetyl CoA or acetyl phosphate in vitro [2123]. To separate protein acetylation from phosphorylation functions, we chose to examine acetyl CoA as acetyl donor.…”
Section: Discussionmentioning
confidence: 99%
“…Under both of these growth conditions, acetyl phosphate is undetectable by the time the cultures reach stationary phase. Taken together, these observations suggested that E. coli cells growing in TB7-glucose acetylate their proteins during stationary phase because that is when glucose is converted to acetyl phosphate, the primary acetyl donor in E. coli (1,2).…”
mentioning
confidence: 80%
“…Under these growth conditions, the cells acetylate their proteins during stationary phase (1)(2)(3). This glucose-induced acetylation is due primarily to production of acetyl phosphate (1,2), a metabolic intermediate of the acetate fermentation pathway (4).…”
mentioning
confidence: 99%
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