In <i>Salmonella</i> Typhimurium and <i>Bacillus subtilis</i>, Nucleoid-Associated HU Proteins Are <i>N</i>-Terminally Acetylated
Here we report that the <i>Salmonella</i> Typhimurium NatB (<i>Se</i>NatB) protein <i>N</i>-terminal acetyltransferase acetylated the <i>N</i>-terminal methionine of the nucleoid-associated HU proteins. Our findings were supported by an in vitro analys...
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2025-06-01
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| author | Anastacia R. Parks Jessica L. Will Liju G. Mathew Sébastien Massier Julie Hardouin Jorge C. Escalante-Semerena |
| author_facet | Anastacia R. Parks Jessica L. Will Liju G. Mathew Sébastien Massier Julie Hardouin Jorge C. Escalante-Semerena |
| author_sort | Anastacia R. Parks |
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| description | Here we report that the <i>Salmonella</i> Typhimurium NatB (<i>Se</i>NatB) protein <i>N</i>-terminal acetyltransferase acetylated the <i>N</i>-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 <i>hilA</i> promoter. <i>Se</i>NatB 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 <i>Se</i>NatB. These results demonstrate that the <i>Se</i>HU proteins are bona fide substrates for the methionine sulfoxide reductases MsrA and MsrB. Finally, we showed that the <i>Bacillus subtilis</i> acetyltransferase, YfmK, is a functional homolog of <i>Se</i>NatB, and that <i>Bs</i>YfmK acetylates the <i>N<sup>α</sup></i> amino group of the initiating methionine of the <i>B. subtilis</i> HU protein (HBsu). |
| format | Article |
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| institution | Kabale University |
| issn | 2076-0817 |
| language | English |
| publishDate | 2025-06-01 |
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| spelling | doaj-art-72db67eefd6542ebab07255fe36351e32025-08-20T03:32:27ZengMDPI AGPathogens2076-08172025-06-0114761610.3390/pathogens14070616In <i>Salmonella</i> Typhimurium and <i>Bacillus subtilis</i>, Nucleoid-Associated HU Proteins Are <i>N</i>-Terminally AcetylatedAnastacia R. Parks0Jessica L. Will1Liju G. Mathew2Sébastien Massier3Julie Hardouin4Jorge C. Escalante-Semerena5Department of Microbiology, University of Georgia, Athens, GA 30602, USADepartment of Microbiology, University of Georgia, Athens, GA 30602, USADepartment of Microbiology, University of Georgia, Athens, GA 30602, USAUniversity of Rouen Normandie, INSA Rouen Normandie, CNRS, Polymers, Biopolymers, Surfaces Laboratory UMR 6270, F-76000 Rouen, FranceUniversity of Rouen Normandie, INSA Rouen Normandie, CNRS, Polymers, Biopolymers, Surfaces Laboratory UMR 6270, F-76000 Rouen, FranceDepartment of Microbiology, University of Georgia, Athens, GA 30602, USAHere we report that the <i>Salmonella</i> Typhimurium NatB (<i>Se</i>NatB) protein <i>N</i>-terminal acetyltransferase acetylated the <i>N</i>-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 <i>hilA</i> promoter. <i>Se</i>NatB 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 <i>Se</i>NatB. These results demonstrate that the <i>Se</i>HU proteins are bona fide substrates for the methionine sulfoxide reductases MsrA and MsrB. Finally, we showed that the <i>Bacillus subtilis</i> acetyltransferase, YfmK, is a functional homolog of <i>Se</i>NatB, and that <i>Bs</i>YfmK acetylates the <i>N<sup>α</sup></i> amino group of the initiating methionine of the <i>B. subtilis</i> HU protein (HBsu).https://www.mdpi.com/2076-0817/14/7/616posttranslational modification<i>N</i>-terminal acetylationHU proteinGram-negative bacteriaGram-positive bacteriaprotein acetylatransferase |
| spellingShingle | Anastacia R. Parks Jessica L. Will Liju G. Mathew Sébastien Massier Julie Hardouin Jorge C. Escalante-Semerena In <i>Salmonella</i> Typhimurium and <i>Bacillus subtilis</i>, Nucleoid-Associated HU Proteins Are <i>N</i>-Terminally Acetylated Pathogens posttranslational modification <i>N</i>-terminal acetylation HU protein Gram-negative bacteria Gram-positive bacteria protein acetylatransferase |
| title | In <i>Salmonella</i> Typhimurium and <i>Bacillus subtilis</i>, Nucleoid-Associated HU Proteins Are <i>N</i>-Terminally Acetylated |
| title_full | In <i>Salmonella</i> Typhimurium and <i>Bacillus subtilis</i>, Nucleoid-Associated HU Proteins Are <i>N</i>-Terminally Acetylated |
| title_fullStr | In <i>Salmonella</i> Typhimurium and <i>Bacillus subtilis</i>, Nucleoid-Associated HU Proteins Are <i>N</i>-Terminally Acetylated |
| title_full_unstemmed | In <i>Salmonella</i> Typhimurium and <i>Bacillus subtilis</i>, Nucleoid-Associated HU Proteins Are <i>N</i>-Terminally Acetylated |
| title_short | In <i>Salmonella</i> Typhimurium and <i>Bacillus subtilis</i>, Nucleoid-Associated HU Proteins Are <i>N</i>-Terminally Acetylated |
| title_sort | in i salmonella i typhimurium and i bacillus subtilis i nucleoid associated hu proteins are i n i terminally acetylated |
| topic | posttranslational modification <i>N</i>-terminal acetylation HU protein Gram-negative bacteria Gram-positive bacteria protein acetylatransferase |
| url | https://www.mdpi.com/2076-0817/14/7/616 |
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