Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 385, Issue 5, Pages 1433-1444Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2008.12.017
Keywords
light-oxygen-voltage; Per-Arnt-Sim; photosensor; protein design; reprogramming of signal specificity
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Funding
- NIGMS NIH HHS [R37 GM036452, R01 GM036452, GM036452] Funding Source: Medline
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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 photosensor domain, Illumination of the resultant fusion kinase YF1 reduced net kinase activity by similar to 1000-fold in vitro. YF1 also controls gene expression in a light-dependent manner in vivo. Signals are transmitted from the light-oxygen-voltage sensor domain to the histidine kinase domain via a 40 degrees-60 degrees rotational movement within an alpha-helical coiled-coil linker; light is acting as a rotary switch. These signaling principles are broadly applicable to domains linked by alpha-helices and to chemo- and photosensors. Conserved sequence motifs, guide the rational design of light-regulated variants of histidine kinases and other proteins. Published by Elsevier Ltd.
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