Title |
[MINIREVIEW]Regulation of gene expression by protein lysine acetylation in Salmonella |
Author |
Hyojeong Koo1†, Shinae Park1†, Min-Kyu Kwak2*, and Jung-Shin Lee1* |
Address |
1Department of Molecular Bioscience, College of Biomedical Science, Kangwon National University, Chuncheon 24341, Republic of Korea, 2Department of Food and Nutrition, College of Human Industry, Eulji University, Seongnam 13135, Republic of Korea |
Bibliography |
Journal of Microbiology, 58(12),979–987, 2020,
|
DOI |
10.1007/s12275-020-0483-8
|
Key Words |
Salmonella, protein lysine acetylation, pathogenicity,
nucleoid-associated protein, histone-like protein |
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. |