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Novel Thermostable Flavin‐binding Fluorescent Proteins from Thermophilic Organisms
Author(s) -
Wingen Marcus,
Jaeger KarlErich,
Gensch Thomas,
Drepper Thomas
Publication year - 2017
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/php.12740
Subject(s) - thermophile , thermostability , flavin group , fluorescence , metagenomics , bacteria , biology , biochemistry , genome , gene , chemistry , computational biology , genetics , enzyme , physics , quantum mechanics
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.