Leveraging the histidine kinase-phosphatase duality to sculpt two-component signaling.
Autor: | Meier SSM; Department of Biochemistry, University of Bayreuth, Bayreuth, Germany., Multamäki E; Department of Anatomy, University of Helsinki, Helsinki, Finland., Ranzani AT; Department of Biochemistry, University of Bayreuth, Bayreuth, Germany., Takala H; Department of Anatomy, University of Helsinki, Helsinki, Finland. heikki.p.takala@jyu.fi.; Department of Biological and Environmental Science, Nanoscience Center, University of Jyvaskyla, Jyvaskyla, Finland. heikki.p.takala@jyu.fi., Möglich A; Department of Biochemistry, University of Bayreuth, Bayreuth, Germany. andreas.moeglich@uni-bayreuth.de.; Bayreuth Center for Biochemistry & Molecular Biology, Universität Bayreuth, Bayreuth, Germany. andreas.moeglich@uni-bayreuth.de.; North-Bavarian NMR Center, Universität Bayreuth, Bayreuth, Germany. andreas.moeglich@uni-bayreuth.de. |
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Jazyk: | angličtina |
Zdroj: | Nature communications [Nat Commun] 2024 Jun 10; Vol. 15 (1), pp. 4876. Date of Electronic Publication: 2024 Jun 10. |
DOI: | 10.1038/s41467-024-49251-8 |
Abstrakt: | Bacteria must constantly probe their environment for rapid adaptation, a crucial need most frequently served by two-component systems (TCS). As one component, sensor histidine kinases (SHK) control the phosphorylation of the second component, the response regulator (RR). Downstream responses hinge on RR phosphorylation and can be highly stringent, acute, and sensitive because SHKs commonly exert both kinase and phosphatase activity. With a bacteriophytochrome TCS as a paradigm, we here interrogate how this catalytic duality underlies signal responses. Derivative systems exhibit tenfold higher red-light sensitivity, owing to an altered kinase-phosphatase balance. Modifications of the linker intervening the SHK sensor and catalytic entities likewise tilt this balance and provide TCSs with inverted output that increases under red light. These TCSs expand synthetic biology and showcase how deliberate perturbations of the kinase-phosphatase duality unlock altered signal-response regimes. Arguably, these aspects equally pertain to the engineering and the natural evolution of TCSs. (© 2024. The Author(s).) |
Databáze: | MEDLINE |
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