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      Regulation of gene expression by protein lysine acetylation in Salmonella

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      https://www.riss.kr/link?id=A107135822

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      다국어 초록 (Multilingual 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.
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      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...

      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.

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      참고문헌 (Reference)

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      5 Schmidt, A., "The quantitative and condition-dependent Escherichia coli proteome" 34 : 104-110, 2016

      6 Groisman, E. A., "The pleiotropic two-component regulatory system PhoP-PhoQ" 183 : 1835-1842, 2001

      7 McFarland, K. A., "The leucine-responsive regulatory protein, Lrp, activates transcription of the fim operon in Salmonella enterica serovar Typhimurium via the fimZ regulatory gene" 190 : 602-612, 2008

      8 Lynch, M., "The bioenergetic costs of a gene" 112 : 15690-15695, 2015

      9 Qin, R., "The bacterial two-hybrid system uncovers the involvement of acetylation in regulating of Lrp activity in Salmonella Typhimurium" 7 : 1864-, 2016

      10 Bienert, S., "The SWISS-MODEL Repository–new features and functionality" 45 : D313-D319, 2017

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      34 Macek, B., "Protein post-translational modifications in bacteria" 17 : 651-664, 2019

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      37 VanDrisse, C. M., "Protein acetylation in bacteria" 73 : 111-132, 2019

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      53 McBrian, M. A., "Histone acetylation regulates intracellular pH" 49 : 310-321, 2013

      54 Bustamante, V. H., "HilD-mediated transcriptional cross-talk between SPI-1 and SPI-2" 105 : 14591-14596, 2008

      55 Banda, M. M., "HilD induces expression of a novel Salmonella Typhimurium invasion factor, YobH, through a regulatory cascade involving SprB" 9 : 12725-, 2019

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      57 Dorman, C. J, "H-NS, the genome sentinel" 5 : 157-161, 2007

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      75 Hu, L. I., "Acetylation of the response regulator RcsB controls transcription from a small RNA promoter" 195 : 4174-4186, 2013

      76 Wang, Q., "Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux" 327 : 1004-1007, 2010

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      81 Verdin, E., "50 years of protein acetylation: from gene regulation to epigenetics, metabolism and beyond" 16 : 258-264, 2015

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