Abstract
Protein lysine acetylation influences many physiological functions,
such as gene regulation, metabolism, and disease in
eukaryotes. Although little is known about the role of lysine
acetylation in bacteria, several reports have proposed its importance
in various cellular processes. Here, we discussed the
function of the protein lysine acetylation and the post-translational
modifications (PTMs) of histone-like proteins in bacteria
focusing on Salmonella pathogenicity. The protein lysine
residue in Salmonella is acetylated by the Pat-mediated enzymatic
pathway or by the acetyl phosphate-mediated non-enzymatic
pathway. In Salmonella, the acetylation of lysine 102
and lysine 201 on PhoP inhibits its protein activity and DNAbinding,
respectively. Lysine acetylation of the transcriptional
regulator, HilD, also inhibits pathogenic gene expression.
Moreover, it has been reported that the protein acetylation
patterns significantly differ in the drug-resistant and
-sensitive Salmonella strains. In addition, nucleoid-associated
proteins such as histone-like nucleoid structuring protein
(H-NS) are critical for the gene silencing in bacteria, and
PTMs in H-NS also affect the gene expression. In this review,
we suggest that protein lysine acetylation and the post-translational
modifications of H-NS are important factors in understanding
the regulation of gene expression responsible
for pathogenicity in Salmonella.
Citations
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