Novel thermostable flavin-binding fluorescent proteins from thermophilic orgamisms
Wingen M, Jaeger K, Gensch T, Drepper T. 2017. Novel thermostable flavin-binding fluorescent proteins from thermophilic orgamisms. Photochemistry and Photobiology. 93(3):849-856
Flavin-binding fluorescent proteins (FbFPs) are small, oxygen-independent in vivo reporters, derived from Light Oxygen Voltage (LOV) domains of photoreceptors. Here, we investigated the thermostability of existing, as well as novel FbFPs, whose genes were identified in genome sequences of various thermophilic bacteria as well as metagenomic libraries from hot springs in the Yellowstone National Park. Detailed in vitro analyses revealed that two of those fluorescent reporter proteins were highly thermostable, exhibiting melting temperatures above 75°C.
- Type
- Journal Article
- Authors
- Wingen, Marcus; Jaeger, Karl-Erich; Gensch, Thomas; Drepper, Thomas
- Units
- YELL
- Keywords
- FbFPs, hot springs, in vitro analyses, LOV, photoreceptors, thermostability
- Subjects
- Ecological Framework: Geology and Soils | Subsurface Geologic Processes | Geothermal Features and Processes