scholarly journals Erratum: Corrigendum: A dark green fluorescent protein as an acceptor for measurement of Förster resonance energy transfer

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Hideji Murakoshi ◽  
Akihiro C. E. Shibata ◽  
Yoshihisa Nakahata ◽  
Junichi Nabekura
Keyword(s):  
Energy Transfer ◽  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Forster Resonance Energy Transfer ◽  
Förster Resonance Energy Transfer ◽  
Dark Green ◽  
Green Fluorescent ◽  
Förster Resonance

Restricted State Selection in Fluorescent Protein Förster Resonance Energy Transfer

2013 ◽  
Vol 135 (21) ◽  
pp. 7883-7890 ◽  
Author(s):  
Thomas A. Masters ◽  
Richard J. Marsh ◽  
Daven A. Armoogum ◽  
Nick Nicolaou ◽  
Banafshé Larijani ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Fluorescent Protein ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Forster Resonance Energy Transfer ◽  
Förster Resonance Energy Transfer ◽  
State Selection ◽  
Förster Resonance

scholarly journals A dark green fluorescent protein as an acceptor for measurement of Förster resonance energy transfer

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Hideji Murakoshi ◽  
Akihiro C. E. Shibata ◽  
Yoshihisa Nakahata ◽  
Junichi Nabekura
Keyword(s):  
Energy Transfer ◽  
Green Fluorescent Protein ◽  
Fluorescence Lifetime ◽  
Fluorescent Protein ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Response Signal ◽  
Dark Green ◽  
Green Fluorescent ◽  
Cell To Cell Variability

Abstract Measurement of Förster resonance energy transfer by fluorescence lifetime imaging microscopy (FLIM-FRET) is a powerful method for visualization of intracellular signaling activities such as protein-protein interactions and conformational changes of proteins. Here, we developed a dark green fluorescent protein (ShadowG) that can serve as an acceptor for FLIM-FRET. ShadowG is spectrally similar to monomeric enhanced green fluorescent protein (mEGFP) and has a 120-fold smaller quantum yield. When FRET from mEGFP to ShadowG was measured using an mEGFP-ShadowG tandem construct with 2-photon FLIM-FRET, we observed a strong FRET signal with low cell-to-cell variability. Furthermore, ShadowG was applied to a single-molecule FRET sensor to monitor a conformational change of CaMKII and of the light oxygen voltage (LOV) domain in HeLa cells. These sensors showed reduced cell-to-cell variability of both the basal fluorescence lifetime and response signal. In contrast to mCherry- or dark-YFP-based sensors, our sensor allowed for precise measurement of individual cell responses. When ShadowG was applied to a separate-type Ras FRET sensor, it showed a greater response signal than did the mCherry-based sensor. Furthermore, Ras activation and translocation of its effector ERK2 into the nucleus could be observed simultaneously. Thus, ShadowG is a promising FLIM-FRET acceptor.

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