Acetylome is Shaped by Lysine Deacetylase Bkd1.

Post-translational modifications of proteins enable swift physiological adaptation of cells to altered growth conditions and stress. Aside from protein phosphorylation, acetylation on ε-amino groups of lysine residues (-ε-lysine acetylation) represents another important post-translational modification of proteins. For many bacterial pathogens, including the whooping cough agent , the role and extent of protein acetylation remain to be defined. We expressed in the BP0960 and BP3063 genes encoding two putative deacetylases of and show that BP0960 encodes a lysine deacetylase enzyme, named Bkd1, that regulates acetylation of a range of proteins. Comparison of the proteome and acetylome of a Δ mutant with the proteome and acetylome of wild-type (PRIDE ID. PXD016384) revealed that acetylation on lysine residues may modulate activities or stabilities of proteins involved in bacterial metabolism and histone-like proteins. However, increased acetylation of the BvgA response regulator protein of the master virulence-regulating BvgAS two-component system affected neither the total levels of produced BvgA nor its phosphorylation status. Indeed, the Δ mutant was not impaired in the production of key virulence factors and its survival within human macrophages was not affected. The Δ mutant exhibited an increased growth rate under carbon source-limiting conditions and its virulence in the mouse lung infection model was somewhat affected. These results indicate that the lysine deacetylase Bkd1 and -ε-lysine acetylation primarily modulate the general metabolism rather than the virulence of .