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Improving FRET dynamic range with bright green and red fluorescent proteins

Nature methods, 2012-10, Vol.9 (10), p.1005-1012 [Peer Reviewed Journal]

COPYRIGHT 2012 Nature Publishing Group ;Copyright Nature Publishing Group Oct 2012 ;ISSN: 1548-7091 ;EISSN: 1548-7105 ;DOI: 10.1038/nmeth.2171 ;PMID: 22961245

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Title:
Improving FRET dynamic range with bright green and red fluorescent proteins
Author: Lam, Amy J ; St-Pierre, François ; Gong, Yiyang ; Marshall, Jesse D ; Cranfill, Paula J ; Baird, Michelle A ; McKeown, Michael R ; Wiedenmann, Jörg ; Davidson, Michael W ; Schnitzer, Mark J ; Tsien, Roger Y ; Lin, Michael Z
Subjects: Base Sequence ; Biochemistry ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism ; Cellular biology ; Cyclic AMP-Dependent Protein Kinases - metabolism ; Fluorescence ; Fluorescence microscopy ; Fluorescence Resonance Energy Transfer - methods ; Fluorescent proteins ; Genetic aspects ; Green Fluorescent Proteins - chemistry ; HEK293 Cells ; HeLa Cells ; Humans ; Luminescent Proteins - chemistry ; Luminescent Proteins - metabolism ; Methods ; Molecular Sequence Data ; Neurons ; Properties ; Proteins ; Red Fluorescent Protein ; rhoA GTP-Binding Protein - metabolism
Is Part Of: Nature methods, 2012-10, Vol.9 (10), p.1005-1012
Description: A variety of genetically encoded reporters use changes in fluorescence (or Förster) resonance energy transfer (FRET) to report on biochemical processes in living cells. The standard genetically encoded FRET pair consists of CFPs and YFPs, but many CFP-YFP reporters suffer from low FRET dynamic range, phototoxicity from the CFP excitation light and complex photokinetic events such as reversible photobleaching and photoconversion. We engineered two fluorescent proteins, Clover and mRuby2, which are the brightest green and red fluorescent proteins to date and have the highest Förster radius of any ratiometric FRET pair yet described. Replacement of CFP and YFP with these two proteins in reporters of kinase activity, small GTPase activity and transmembrane voltage significantly improves photostability, FRET dynamic range and emission ratio changes. These improvements enhance detection of transient biochemical events such as neuronal action-potential firing and RhoA activation in growth cones.
Publisher: United States: Nature Publishing Group
Language: English
Identifier: ISSN: 1548-7091
EISSN: 1548-7105
DOI: 10.1038/nmeth.2171
PMID: 22961245
Source: MEDLINE
ProQuest Central

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Improving FRET dynamic range with bright green and red fluorescent proteins

COPYRIGHT 2012 Nature Publishing Group ;Copyright Nature Publishing Group Oct 2012 ;ISSN: 1548-7091 ;EISSN: 1548-7105 ;DOI: 10.1038/nmeth.2171 ;PMID: 22961245

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