Structural and functional characterization of MrpR, the master repressor of the Bacillus subtilis prophage SPβ.
Autor: | Kohm K; FG Synthetic Microbiology, Institute for Biotechnology, BTU Cottbus-Senftenberg, Senftenberg, Germany.; FG Molecular Microbiology, Institute for Biology, University of Hohenheim, Stuttgart, Germany., Jalomo-Khayrova E; Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry, Phillips-University Marburg, Marburg, Germany., Krüger A; Institute of Bio- and Geosciences, iBG-1: Biotechnology, FZ Jülich, Germany., Basu S; FG Synthetic Microbiology, Institute for Biotechnology, BTU Cottbus-Senftenberg, Senftenberg, Germany., Steinchen W; Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry, Phillips-University Marburg, Marburg, Germany., Bange G; Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry, Phillips-University Marburg, Marburg, Germany.; Max-Planck Institute for Terrestrial Microbiology, Marburg, Germany., Frunzke J; Institute of Bio- and Geosciences, iBG-1: Biotechnology, FZ Jülich, Germany., Hertel R; FG Synthetic Microbiology, Institute for Biotechnology, BTU Cottbus-Senftenberg, Senftenberg, Germany.; Department of Genomic and Applied Microbiology, Institute of Microbiology and Genetics, Georg-August-University of Göttingen, Göttingen, Germany., Commichau FM; FG Synthetic Microbiology, Institute for Biotechnology, BTU Cottbus-Senftenberg, Senftenberg, Germany.; FG Molecular Microbiology, Institute for Biology, University of Hohenheim, Stuttgart, Germany., Czech L; Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry, Phillips-University Marburg, Marburg, Germany. |
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Jazyk: | angličtina |
Zdroj: | Nucleic acids research [Nucleic Acids Res] 2023 Sep 22; Vol. 51 (17), pp. 9452-9474. |
DOI: | 10.1093/nar/gkad675 |
Abstrakt: | Prophages control their lifestyle to either be maintained within the host genome or enter the lytic cycle. Bacillus subtilis contains the SPβ prophage whose lysogenic state depends on the MrpR (YopR) protein, a key component of the lysis-lysogeny decision system. Using a historic B. subtilis strain harboring the heat-sensitive SPβ c2 mutant, we demonstrate that the lytic cycle of SPβ c2 can be induced by heat due to a single nucleotide exchange in the mrpR gene, rendering the encoded MrpRG136E protein temperature-sensitive. Structural characterization revealed that MrpR is a DNA-binding protein resembling the overall fold of tyrosine recombinases. MrpR has lost its recombinase function and the G136E exchange impairs its higher-order structure and DNA binding activity. Genome-wide profiling of MrpR binding revealed its association with the previously identified SPbeta repeated element (SPBRE) in the SPβ genome. MrpR functions as a master repressor of SPβ that binds to this conserved element to maintain lysogeny. The heat-inducible excision of the SPβ c2 mutant remains reliant on the serine recombinase SprA. A suppressor mutant analysis identified a previously unknown component of the lysis-lysogeny management system that is crucial for the induction of the lytic cycle of SPβ. (© The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.) |
Databáze: | MEDLINE |
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