Journal Article

FZJ-2017-03599

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Novel Thermostable Flavin-binding Fluorescent Proteins from Thermophilic Organisms

Wingen, M.FZJ* ; Jaeger, K.-E.FZJ* ; Gensch, T. (Corresponding author)FZJ* ; Drepper, T.FZJ*

2017
Wiley-Blackwell Malden, Mass.

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Please use a persistent id in citations: 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.

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Contributing Institute(s):

1. Zelluläre Biophysik (ICS-4)
2. Institut für Molekulare Enzymtechnologie (HHUD) (IMET)

Research Program(s):

1. 552 - Engineering Cell Function (POF3-552) (POF3-552)
2. 581 - Biotechnology (POF3-581) (POF3-581)

Appears in the scientific report 2017

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Database coverage:
; BIOSIS Previews ; Current Contents - Life Sciences ; Ebsco Academic Search ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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