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Review
. 2011 Apr;14(2):200-4.
doi: 10.1016/j.mib.2010.12.013. Epub 2011 Jan 14.

Control of protein function by reversible Nɛ-lysine acetylation in bacteria

Sandy Thao  1 , Jorge C Escalante-Semerena
Affiliations
Review

Control of protein function by reversible Nɛ-lysine acetylation in bacteria

Sandy Thao et al. Curr Opin Microbiol. 2011 Apr.

Abstract

Recently published work indicates that reversible N(ɛ)-lysine (N(ɛ)-Lys) acetylation of proteins in bacteria may be as diverse, and as important for cellular function, as it has been reported in eukaryotes for the last five decades. In addition to biochemical and genetic approaches, proteomic studies have identified N(ɛ)-Lys acetylation of proteins and enzymes involved in diverse cellular activities such as transcription, translation, stress response, detoxification, and especially carbohydrate and energy metabolism. These findings provide a platform for elucidating the molecular mechanisms behind modulation of enzyme activity by N(ɛ)-Lys acetylation, as well as for understanding how the prokaryotic cell maintains homeostasis in a changing environment.

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Figures

Figure 1
Figure 1. Proposed mechanism of GNAT-catalyzed acetyl transfer
Biochemical and structural evidence suggest that the GNAT family of HATs use a sequential mechanism of acetyl transfer. In this mechanism, Ac-CoA binds first, followed by the other substrate to form a ternary complex. The target lysine is deprotonated by an active site residue acting as a base, triggering a nucleophilic attack on the carbonyl carbon of Ac-CoA. Figure is adapted from Berndsen and Denu [42]. The acetyl group is highlighted in blue; E = enzyme; S = substrate.
Figure 2
Figure 2. Posttranslational regulation of Acs activity by Ac-CoA-dependent Pat acetylation
Acetate cannot be utilized by the cell until it is converted to the high-energy intermediate, Ac-CoA. Acs (AMP-forming; EC 6.2.1.1) converts acetate to Ac-CoA via two half-reactions. In the first half-reaction, Acs converts acetate and ATP to the enzyme-bound intermediate acetyladenylate (Ac-AMP). In the second half-reaction, Acs reacts Ac-AMP with CoASH to form Ac-CoA, releasing AMP. Pat inactivates Acs by acetylation of an active site lysine, Lys609, preventing catalysis of the first half-reaction.
Figure 3
Figure 3. Graphical representation of metabolic targets identified by two proteomic studies
A. The majority of the Nε-Lys acetylation modifications [125 acetylation sites in 85 proteins (left), and 138 acetylation sites in 91 proteins (right)] were identified in enzymes involved in metabolism. B. Of the ~40 targets shared by both studies, only 6 targets shared consensus on the site(s) assigned as acetylated.
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