Regulation of gene expression by protein lysine acetylation in Salmonella
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MINIREVIEW Regulation of gene expression by protein lysine acetylation in Salmonella Hyojeong Koo1†, Shinae Park1†, Min-Kyu Kwak2*, and Jung-Shin Lee1* 1 Department of Molecular Bioscience, College of Biomedical Science, Kangwon National University, Chuncheon 24341, Republic of Korea 2 Department of Food and Nutrition, College of Human Industry, Eulji University, Seongnam 13135, Republic of Korea
(Received Sep 18, 2020 / Revised Oct 12, 2020 / Accepted Oct 12, 2020)
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. Keywords: Salmonella, protein lysine acetylation, pathogenicity, nucleoid-associated protein, histone-like protein
† These authors contributed equally to this work. *For correspondence. (J. S. Lee) E-mail: [email protected]; Tel.: +82-33-250-8549; Fax: +82-33-259-5641 / (M. K. Kwak) E-mail: genie6 @eulji.ac.kr; Tel.: +82-31-740-7418 Copyright G2020, The Microbiological Society of Korea
Introduction Salmonella enterica is a Gram-negative facultative pathogen that causes a range of diseases, from mild gastroenteritis to severe systemic infection, in a variety of animal hosts (Hurley et al., 2014; Kurtz et al., 2017). More than 2,500 Salmonella serotypes have been identified so far, and Salmonella causes 155,000 deaths per year (Eng et al., 2015). Salmonella has distinct gene clusters known as, Salmonella pathogenicity islands (SPIs) that are located on the chromosomal DNA and encode for Type III secretion systems (T3SS) (Hansen-Wester and Hensel, 2001). SPI-1 is involved in the invasion of Salmonella into nonphagocytic cells, while SPI-2 is associated with the survival and proliferation of Salmonella in the host pha
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