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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Main Authors: Anastacia R. Parks, Jessica L. Will, Liju G. Mathew, Sébastien Massier, Julie Hardouin, Jorge C. Escalante-Semerena
Format: Article
Language:English
Published: MDPI AG 2025-06-01
Series:Pathogens
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Online Access:https://www.mdpi.com/2076-0817/14/7/616
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Summary: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).
ISSN:2076-0817