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Pathogens
Volume 14
Issue 7
10.3390/pathogens14070616
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This is an early access version, the complete PDF, HTML, and XML versions will be available soon.
Article

In Salmonella Typhimurium and Bacillus subtilis, Nucleoid-Associated HU Proteins Are N-Terminally Acetylated

by
Anastacia R. Parks
1,
Jessica L. Will
1,
Liju G. Mathew
1,
Sébastien Massier
2,
Julie Hardouin
2,3 and
Jorge C. Escalante-Semerena
1,*
1
Department of Microbiology, University of Georgia, Athens, GA 30602, USA
2
University of Rouen Normandie, INSA Rouen Normandie, CNRS, Polymers, Biopolymers, Surfaces Laboratory UMR 6270, F-76000 Rouen, France
3
3 Université de Rouen Normandie, INSERM US 51 CNRS UAR 2026, HeRacLeS-PISSARO, Normandie Université, 76000 Rouen, France
*
Author to whom correspondence should be addressed.
Pathogens 2025, 14(7), 616; https://doi.org/10.3390/pathogens14070616
Submission received: 28 April 2025 / Revised: 12 June 2025 / Accepted: 14 June 2025 / Published: 20 June 2025
(This article belongs to the Special Issue Post-translational Modifications, a Powerful Mechanism for Bacterial Life and Survival)
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Abstract

Here we report that the Salmonella Typhimurium NatB (SeNatB) protein N-terminal acetyltransferase acetylated the N-terminal methionine of the nucleoid-associated HU proteins. Our findings were supported by an in vitro analysis of acetylation of the HUα and HUβ proteins and lysine-null (K-null) variants, and by an in vivo analysis of the effect of acetylation on HU-mediated transcriptional regulation of a known target of HU, the hilA promoter. SeNatB did not acetylate the initiating methionines of HU proteins that were oxidized to methionine sulfoxide, but the reduction of these methionine sulfoxide residues restored the acetylation of HU proteins by SeNatB. These results demonstrate that the SeHU proteins are bona fide substrates for the methionine sulfoxide reductases MsrA and MsrB. Finally, we showed that the Bacillus subtilis acetyltransferase, YfmK, is a functional homolog of SeNatB, and that BsYfmK acetylates the Nα amino group of the initiating methionine of the B. subtilis HU protein (HBsu).
Keywords: posttranslational modification; N-terminal acetylation; Hu protein; Gram-negative bacteria; Gram-positive bacteria; protein acetylatransferase; Salmonellla pathogenesis posttranslational modification; N-terminal acetylation; Hu protein; Gram-negative bacteria; Gram-positive bacteria; protein acetylatransferase; Salmonellla pathogenesis
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MDPI and ACS Style

Parks, A.R.; Will, J.L.; Mathew, L.G.; Massier, S.; Hardouin, J.; Escalante-Semerena, J.C. In Salmonella Typhimurium and Bacillus subtilis, Nucleoid-Associated HU Proteins Are N-Terminally Acetylated. Pathogens 2025, 14, 616. https://doi.org/10.3390/pathogens14070616

AMA Style

Parks AR, Will JL, Mathew LG, Massier S, Hardouin J, Escalante-Semerena JC. In Salmonella Typhimurium and Bacillus subtilis, Nucleoid-Associated HU Proteins Are N-Terminally Acetylated. Pathogens. 2025; 14(7):616. https://doi.org/10.3390/pathogens14070616

Chicago/Turabian Style

Parks, Anastacia R., Jessica L. Will, Liju G. Mathew, Sébastien Massier, Julie Hardouin, and Jorge C. Escalante-Semerena. 2025. "In Salmonella Typhimurium and Bacillus subtilis, Nucleoid-Associated HU Proteins Are N-Terminally Acetylated" Pathogens 14, no. 7: 616. https://doi.org/10.3390/pathogens14070616

APA Style

Parks, A. R., Will, J. L., Mathew, L. G., Massier, S., Hardouin, J., & Escalante-Semerena, J. C. (2025). In Salmonella Typhimurium and Bacillus subtilis, Nucleoid-Associated HU Proteins Are N-Terminally Acetylated. Pathogens, 14(7), 616. https://doi.org/10.3390/pathogens14070616

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