Functional diversification despite structural congruence in the HipBST toxin-antitoxin system of Legionella pneumophila .

Autor: Lin JD; Department of Molecular Genetics, University of Toronto , Toronto, Ontario, Canada., Stogios PJ; Department of Chemical Engineering and Applied Chemistry, University of Toronto , Toronto, Ontario, Canada., Abe KT; Department of Molecular Genetics, University of Toronto , Toronto, Ontario, Canada.; Lunenfeld-Tanenbaum Research Institute, Sinai Health , Toronto, Ontario, Canada., Wang A; Department of Molecular Genetics, University of Toronto , Toronto, Ontario, Canada., MacPherson J; Department of Molecular Genetics, University of Toronto , Toronto, Ontario, Canada., Skarina T; Department of Chemical Engineering and Applied Chemistry, University of Toronto , Toronto, Ontario, Canada., Gingras A-C; Department of Molecular Genetics, University of Toronto , Toronto, Ontario, Canada.; Lunenfeld-Tanenbaum Research Institute, Sinai Health , Toronto, Ontario, Canada., Savchenko A; Department of Chemical Engineering and Applied Chemistry, University of Toronto , Toronto, Ontario, Canada.; Department of Microbiology, Immunology and Infectious Diseases, University of Calgary , Calgary, Alberta, Canada.; Center for Structural Genomics of Infectious Diseases (CSGID), University of Calgary , Calgary, Alberta, Canada., Ensminger AW; Department of Molecular Genetics, University of Toronto , Toronto, Ontario, Canada.; Department of Biochemistry, University of Toronto , Toronto, Ontario, Canada.
Jazyk: angličtina
Zdroj: MBio [mBio] 2023 Oct 31; Vol. 14 (5), pp. e0151023. Date of Electronic Publication: 2023 Oct 11.
DOI: 10.1128/mbio.01510-23
Abstrakt: Importance: Toxin-antitoxin (TA) systems are parasitic genetic elements found in almost all bacterial genomes. They are exchanged horizontally between cells and are typically poorly conserved across closely related strains and species. Here, we report the characterization of a tripartite TA system in the bacterial pathogen Legionella pneumophila that is highly conserved across Legionella species genomes. This system (denoted HipBST Lp ) is a distant homolog of the recently discovered split-HipA system in Escherichia coli (HipBST Ec ). We present bioinformatic, molecular, and structural analyses of the divergence between these two systems and the functionality of this newly described TA system family. Furthermore, we provide evidence to refute previous claims that the toxin in this system (HipT Lp ) possesses bifunctionality as an L. pneumophila virulence protein. Overall, this work expands our understanding of the split-HipA system architecture and illustrates the potential for undiscovered biology in these abundant genetic elements.
Competing Interests: The authors declare no conflict of interest.
Databáze: MEDLINE
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