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. 2011 Jul 15;410(4):846-51.
doi: 10.1016/j.bbrc.2011.06.076. Epub 2011 Jun 15.

Protein acetylation in prokaryotes increases stress resistance

Qun Ma  1 , Thomas K Wood
Affiliations

Protein acetylation in prokaryotes increases stress resistance

Qun Ma et al. Biochem Biophys Res Commun. .

Abstract

Acetylation of lysine residues is conserved in all three kingdoms; however, its role in prokaryotes is unknown. Here we demonstrate that acetylation enables the reference bacterium Escherichia coli to withstand environmental stress. Specifically, the bacterium reaches higher cell densities and becomes more resistant to heat and oxidative stress when its proteins are acetylated as shown by deletion of the gene encoding acetyltransferase YfiQ and the gene encoding deacetylase CobB as well as by overproducing YfiQ and CobB. Furthermore, we show that the increase in oxidative stress resistance with acetylation is due to the induction of catalase activity through enhanced katG expression. We also found that two-component system proteins CpxA, PhoP, UvrY, and BasR are associated with cell catalase activity and may be responsible as the connection between bacterial acetylation and the stress response. This is the first demonstration of a specific environmental role of acetylation in prokaryotes.

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Figures

Figure 1
Figure 1. Resistance to oxidative and heat stress
E. coli BW25113 wild-type/pCA24N, cobB/pCA24N, cobB/pCA24N_cobB, yfiQ/pCA24N, and yfiQ/pCA24N_yfiQ were tested for H2O2 resistance (A) and heat resistance (B) in LB medium at 37°C.
Figure 2
Figure 2. Catalase activity
E. coli BW25113 wild-type/pCA24N, cobB/pCA24N, cobB/pCA24N_cobB, yfiQ/pCA24N, and yfiQ/pCA24N_yfiQ were compared for their catalase activity using the a spectrophotometric method (A) and a colorimetric method with dicarboxidine/lactoperoxidase (B). Wild-type/pCA24N data are indicated by filled circles, cobB/pCA24N by empty circles, cobB/pCA24N_cobB by filled triangles, yfiQ/pCA24N by empty triangles, and yfiQ/pCA24N_yfiQ by solid squares.
Figure 3
Figure 3. Catalase activity for mutants of two-component systems
Single mutants from seven sets of two-component systems were compared for their catalase activity using the spectrophotometric method. The katE mutant was used as a negative control.
Figure 4
Figure 4. Growth curves
The strains were grown in LB medium with 30 μg/mL chloramphenicol to retain the plasmids at 37°C, and 0.1 mM IPTG was added to induce cobB and yfiQ expression after 2 h. Symbols as defined in Fig. 2B.
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