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• W330245850 abstract "Global protein acetylation is anewly discovered phenomenon in bacteria. Of the more than 250acetylations reported in E. coli, many are of metabolic enzymes.Thus, acetylation could represent a novel posttranslationalmechanism of metabolic control. Yet, almost nothing is known aboutthe regulation of these acetylations or of their metabolicoutcomes. Here, we report that the cAMP receptor protein (CRP)regulates protein acetylation in E. coli and provide evidence thatprotein acetylation modulates the flux of carbon through centralmetabolism. When we grew cells in mixed amino acids supplementedwith glucose and cAMP, global protein acetylation increased in aCRP-dependent manner and several of the acetylated proteins werecentral metabolic enzymes. Much of this CRP-mediated acetylationrequired activation region 1 (AR1), a surface patch that allows CRPto interact with RNA polymerase. A second surface patch (AR2) alsowas involved, albeit to a lesser degree. These results raise thepossibility that CRP might regulate the transcription of a proteinacetyltransferase. Indeed, a recent report suggested that CRP mightregulate transcription of the protein acetyltransferase YfiQ (alsoknown as Pat) by a mechanism that would require AR2. We furtherobtained bioinformatic evidence that supports the hypothesis thatCRP also could regulate yfiQ transcription in an AR1-dependentmanner. Since CRP regulates metabolism, we asked if YfiQ couldinfluence metabolism. Using Phenotype MicroArrayanalysis, we found that a yfiQ null mutant exhibits a distinctivedefect during growth on gluconeogenic carbonsources and a distinct advantage during growth on a carbon sourcethat bypasses the need for gluconeogenesis. In vitro acetylationassays identified four substrates of YfiQ. Three YfiQ substrateswere the strictly irreversible glycolytic enzymes PfkA, PfkB, andLpdA. The fourth was CRP itself. We thus hypothesize that CRPactivates yfiQ transcription, whose protein product acetylates asubset of metabolic enzymes, altering their function and shiftingthe balance between glycolysis and gluconeogenesis. We furtherpropose that YfiQ acetylates CRP. Efforts to determine how thisacetylation affects the CRP-dependent transcriptome areunderway." @default.
• W330245850 created "2016-06-24" @default.
• W330245850 creator A5038422966 @default.
• W330245850 date "2012-01-01" @default.
• W330245850 modified "2023-09-28" @default.
• W330245850 title "Understanding the Regulation of Metabolic Enzyme Acetylation in E. Coli" @default.
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