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Design and Signaling Mechanism of Light-Regulated Histidine Kinases
Open accessAbstract
Signal transduction proteins are organized into sensor (input) domains that perceive a signal and, in response, regulate the biological activity of effector (output) domains. We reprogrammed the input signal specificity of a normally oxygen‐sensitive, light‐inert histidine kinase by replacing its chemosensor domain by a light‐oxygen‐voltage (LOV) photosensor domain. Illumination of the resultant fusion kinase YF1 reduced net kinase activity by ~1000‐fold in vitro. YF1 also controls gene expression in a light‐dependent manner in vivo. Signals are transmitted from the LOV sensor domain to the histidine kinase domain via a 40‐60º rotational movement within an α‐helical coiled coil linker; light is acting as a rotary switch. These signaling principles are broadly applicable to domains linked by α‐helices, and to both chemo‐ and photosensors. Conserved sequence motifs guide the rational design of light‐regulated variants of histidine kinases and other proteins.
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Cites
The HAMP Domain Structure Implies Helix Rotation in Transmembrane Signaling
Hulko, M., Berndt, F., Gruber, M., Linder, J. U., Truffault, V., Schultz, A., Martin, J., Schultz, J. E., Lupas, A. N., & Coles, M. (2006) · Cell · doi:10.1016/j.cell.2006.06.058 · Cited by 416
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Wu, Y. I., Frey, D., Lungu, O. I., Jaehrig, A., Schlichting, I., Kuhlman, B., & Hahn, K. M. (2009) · Nature · doi:10.1038/nature08241 · Cited by 1,083
Evolution of Two-Component Signal Transduction Systems
Capra, E. J., & Laub, M. T. (2012) · Annual Review of Microbiology · doi:10.1146/annurev-micro-092611-150039 · Cited by 705
Molecular Mechanisms of Two-Component Signal Transduction
Zschiedrich, C. P., Keidel, V., & Szurmant, H. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.08.003 · Cited by 540
Structure and function of plant photoreceptors
Möglich, A., Yang, X., Ayers, R. A., & Moffat, K. (2010) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042809-112259 · Cited by 499
Self-citationStierl, M., Stumpf, P., Udwari, D., Gueta, R., Hagedorn, R., Losi, A., Gärtner, W., Petereit, L., Efetova, M., Schwarzel, M., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.185496 · Cited by 422
Metadata
- Authors
- Möglich, A., Ayers, R. A., & Moffat, K.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2009-02
- Volume
- 385
- Issue
- 5
- Pages
- 1433-1444
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W1993744080
- Cited by
- 341
- References
- 1
- FWCI
- 7.64
- Type
- journal article
- Language
- en
- Open access
- green
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- Möglich, A., Ayers, R. A., & Moffat, K. (2009). Design and Signaling Mechanism of Light-Regulated Histidine Kinases. Journal of Molecular Biology. https://doi.org/10.1016/j.jmb.2008.12.017
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