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Regulation of gene expression by protein lysine acetylation in Salmonella

Journal of Microbiology 2020년 58권 12호 p.979 ~ 987
구효정, 박신애, 곽민규, 이정신,
소속 상세정보
구효정 ( Koo Hyo-Jeong ) - Kangwon National University College of Biomedical Sciences Department of Molecular Bioscience
박신애 ( Park Shin-Ae ) - Kangwon National University College of Biomedical Sciences Department of Molecular Bioscience
곽민규 ( Kwak Min-Kyu ) - Eulji University College of Human Industry Department of Food and Nutrition
이정신 ( Lee Jung-Shin ) - Kangwon National University College of Biomedical Sciences Department of Molecular Bioscience

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 DNA-binding, 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.

키워드

Salmonella; protein lysine acetylation; pathogenicity; nucleoid-associated protein; histone-like protein

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