Novel Thermostable Flavin-binding Fluorescent Proteins from Thermophilic Organisms

Photochem Photobiol. 2017 May;93(3):849-856. doi: 10.1111/php.12740.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Flavins / chemistry*
  • Fluorescence

Substances

  • Bacterial Proteins
  • Flavins