H-NS is a bacterial transposon capture protein

Charles Cooper, Simon Legood, Rachel L. Wheat, David Forrest, Prateek Sharma, James R. J. Haycocks and David C. Grainger ()
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Charles Cooper: University of Birmingham
Simon Legood: University of Birmingham
Rachel L. Wheat: University of Birmingham
David Forrest: University of Birmingham
Prateek Sharma: University of Birmingham
James R. J. Haycocks: University of Birmingham
David C. Grainger: University of Birmingham

Nature Communications, 2024, vol. 15, issue 1, 1-15

Abstract: Abstract The histone-like nucleoid structuring (H-NS) protein is a DNA binding factor, found in gammaproteobacteria, with functional equivalents in diverse microbes. Universally, such proteins are understood to silence transcription of horizontally acquired genes. Here, we identify transposon capture as a major overlooked function of H-NS. Using genome-scale approaches, we show that H-NS bound regions are transposition “hotspots”. Since H-NS often interacts with pathogenicity islands, such targeting creates clinically relevant phenotypic diversity. For example, in Acinetobacter baumannii, we identify altered motility, biofilm formation, and interactions with the human immune system. Transposon capture is mediated by the DNA bridging activity of H-NS and, if absent, more ubiquitous transposition results. Consequently, transcribed and essential genes are disrupted. Hence, H-NS directs transposition to favour evolutionary outcomes useful for the host cell.

Date: 2024
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DOI: 10.1038/s41467-024-51407-5

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