H-NS is a bacterial transposon capture protein.

Autor: Cooper C; School of Biosciences, University of Birmingham, Birmingham, UK., Legood S; School of Biosciences, University of Birmingham, Birmingham, UK., Wheat RL; School of Biosciences, University of Birmingham, Birmingham, UK., Forrest D; School of Biosciences, University of Birmingham, Birmingham, UK., Sharma P; School of Biosciences, University of Birmingham, Birmingham, UK., Haycocks JRJ; School of Biosciences, University of Birmingham, Birmingham, UK., Grainger DC; School of Biosciences, University of Birmingham, Birmingham, UK. d.grainger@bham.ac.uk.
Jazyk: angličtina
Zdroj: Nature communications [Nat Commun] 2024 Aug 20; Vol. 15 (1), pp. 7137. Date of Electronic Publication: 2024 Aug 20.
DOI: 10.1038/s41467-024-51407-5
Abstrakt: 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.
(© 2024. The Author(s).)
Databáze: MEDLINE
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