Promiscuity of response regulators for thioredoxin steers bacterial virulence

Author:

Kim Ju-SimORCID,Born Alexandra,Till James Karl A.ORCID,Liu LinORCID,Kant SashiORCID,Henen Morkos A.,Vögeli BeatORCID,Vázquez-Torres Andrés

Abstract

AbstractThe exquisite specificity between a sensor kinase and its cognate response regulator ensures faithful partner selectivity within two-component pairs concurrently firing in a single bacterium, minimizing crosstalk with other members of this conserved family of paralogous proteins. We show that conserved hydrophobic and charged residues on the surface of thioredoxin serve as a docking station for structurally diverse response regulators. Using the OmpR protein, we identify residues in the flexible linker and the C-terminal β-hairpin that enable associations of this archetypical response regulator with thioredoxin, but are dispensable for interactions of this transcription factor to its cognate sensor kinase EnvZ, DNA or RNA polymerase. Here we show that the promiscuous interactions of response regulators with thioredoxin foster the flow of information through otherwise highly dedicated two-component signaling systems, thereby enabling both the transcription of Salmonella pathogenicity island-2 genes as well as growth of this intracellular bacterium in macrophages and mice.

Funder

Division of Intramural Research, National Institute of Allergy and Infectious Diseases

Department of Veterans Affairs | Office of Academic Affiliations, Department of Veterans Affairs

U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry,Multidisciplinary

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