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Leveraging the histidine kinase-phosphatase duality to sculpt two-component signaling

Title data

Meier, Stefanie S. M. ; Multamäki, Elina ; Ranzani, Américo T. ; Takala, Heikki ; Möglich, Andreas:
Leveraging the histidine kinase-phosphatase duality to sculpt two-component signaling.
In: Nature Communications. Vol. 15 (2024) . - 4876.
ISSN 2041-1723
DOI: https://doi.org/10.1038/s41467-024-49251-8

Official URL: Volltext

Project information

Project financing: Deutsche Forschungsgemeinschaft

Abstract in another language

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.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: Protein design; Expression systems; Synthetic biology; Kinases
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry II - Photobiochemistry > Chair Biochemistry II - Photobiochemistry - Univ.-Prof. Dr. Andreas Möglich
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 570 Life sciences, biology
Date Deposited: 24 Jun 2024 11:23
Last Modified: 24 Jun 2024 11:23
URI: https://eref.uni-bayreuth.de/id/eprint/89829