Diversity and evolution of the green fluorescent protein family

Labas, Yulii A.; Gurskaya, Nadya G.; Yanushevich, Yurii G.; Fradkov, Arkady F.; Lukyanov, Konstantin A.; Lukyanov, Sergey; Matz, Mikhail V.

doi:10.1073/pnas.062552299

Cited by 346 publications

(295 citation statements)

References 32 publications

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“…While elucidation of the detailed mechanism of this protective effect is beyond the scope of the present study, the data nevertheless suggest that the antioxidant properties of GFP could be an important supplement to the antioxidant defenses of symbiotic cnidarians under the constant hyperoxic conditions that these organisms experience during the daytime. It would be informative to ascertain whether the diversification of GFPs within the cnidarians, which has resulted in many fluorescent homologs exhibiting different fluorescence properties, and non-fluorescent homologs [3][4][5][6], also have the ability to quench O 2 •− . The fact that corals are hyperoxic, produce large quantities of ROS, and require robust antioxidant protection is well documented [17].…”

Section: Discussionmentioning

confidence: 99%

“…GFP from the hydromedusa Aequorea victoria has been sequenced and is now widely used as a reporter gene for transcriptional studies at the molecular level while mutants from A. victoria and other cnidarians with different fluorescent emission properties from blue to red have also been described [3]. GFP has also been identified in a variety of nonsymbiotic and symbiotic cnidarians including reef-forming corals [4][5][6][7][8] where the protein is not coupled to a bioluminescent system and its function(s) remains unclear. It has been proposed that GFP and their homologues improve the efficiency of photosynthesis or provide photoprotection for the symbiotic dinoflagellates (zooxanthellae) [9].…”

Section: Introductionmentioning

confidence: 99%

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Quenching of superoxide radicals by green fluorescent protein

Bou-Abdallah

Chasteen

Lesser

2006

Biochimica et Biophysica Acta (BBA) - General Subjects

162

144

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Green fluorescent protein (GFP) is a widely used in vivo molecular marker. These proteins are particularly resistant, and maintain function, under a variety of cellular conditions such as pH extremes and elevated temperatures. Green fluorescent proteins are also abundant in several groups of marine invertebrates including reef-forming corals. While molecular oxygen is required for the post-translational maturation of the protein, mature GFPs are found in corals where hyperoxia and reactive oxygen species (ROS) occur due to the photosynthetic activity of algal symbionts. In vitro spin trapping electron paramagnetic resonance and spectrophotometric assays of superoxide dismutase (SOD)-like enzyme activity show that wild type GFP from the hydromedusa, Aequorea victoria, quenches superoxide radicals (O 2 •− ) and exhibits SOD-like activity by competing with cytochrome c for reaction with O 2 •− . When exposed to high amounts of O 2 •− the SOD-like activity and protein structure of GFP are altered without significant changes to the fluorescent properties of the protein. Because of the distribution of fluorescent proteins in both the epithelial and gastrodermal cells of reef-forming corals we propose that GFP, and possibly other fluorescent proteins, can provide supplementary antioxidant protection.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Quenching of superoxide radicals by green fluorescent protein

Bou-Abdallah

Chasteen

Lesser

2006

Biochimica et Biophysica Acta (BBA) - General Subjects

162

144

View full text Add to dashboard Cite

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“…More recently, a new red fluorescent protein (DsRed) that emits fluorescence at 583 nm has been isolated from tropical Discosoma corals [50]. Another red fluorescent protein that is potentially even more suitable for in vivo imaging is HcRed, generated by site-directed and random mutagenesis of a nonfluorescent chromoprotein isolated from the reef coral Heteractis crispa, which emits light at 618 nm [51,52]. Unlike bioluminescent proteins (discussed below), fluorescent proteins do not require cofactors or chemical staining before in vivo imaging.…”

Section: Fluorescent Proteins Amentioning

confidence: 99%

Shedding light onto live molecular targets

Weissleder

Ntziachristos

2003

Nat Med

1,781

1,319

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Abstract-Optical sensing of specific molecular targets and pathways deep inside living mice has become possible as a result of a number of advances. These include design of biocompatible near-infrared fluorochromes, development of targeted and activatable 'smart' imaging probes, engineered photoproteins and advances in photon migration theory and reconstruction. Together, these advances will provide new tools making it possible to understand more fully the functioning of protein networks, diagnose disease earlier and speed along drug discovery.

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“…Cloning of Anthozoa fluorescent proteins, such as red DsRed 13,14 and far-red HcRed 15 , has expanded the in vivo applications of FRET, but a major limitation of Anthozoa proteins for FRET applications is their obligate oligomerization 16 . Recent generation of a monomerized mutant of DsRed, monomeric red fluorescent protein 1 (mRFP) 17 , provides the opportunity to generate functional monomeric fusion proteins and to use mRFP as a FRET acceptor with proteins fused to GFP or its mutants.…”

mentioning

confidence: 99%

Three-chromophore FRET microscopy to analyze multiprotein interactions in living cells

2004

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Nearly every major process in a cell is carried out by assemblies of multiple dynamically interacting protein molecules. To study multi-protein interactions within such molecular machineries, we have developed a fluorescence microscopy method called three-chromophore fluorescence resonance energy transfer . This method allows analysis of three mutually dependent energy transfer processes between the fluorescent labels, such as cyan, yellow and monomeric red fluorescent proteins. Here, we describe both theoretical and experimental approaches that discriminate the parallel versus the sequential energy transfer processes in the 3-FRET system. These approaches were established in vitro and in cultured mammalian cells, using chimeric proteins consisting of two or three fluorescent proteins linked together. The 3-FRET microscopy was further applied to the analysis of three-protein interactions in the constitutive and activation-dependent complexes in single endosomal compartments. These data highlight the potential of 3-FRET microscopy in studies of spatial and temporal regulation of signaling processes in living cells.Many cellular processes are governed by multi-component molecular machineries that rely on dynamic and highly coordinated protein-protein interactions. For example, assembly of protein complexes during signal transduction processes increases the speed of enzymatic reactions, ensures the specificity of signaling and targets signaling molecules to proper intracellular compartments. During recent years, fluorescence resonance energy transfer (FRET) has become a key method for the analysis of proteinprotein interactions during signal transduction in living cells [1][2][3] . FRET studies using proteins tagged with mutant derivatives of the green fluorescent protein (GFP) have demonstrated the formation of complexes of signaling proteins in various intracellular compartments 4-7 . FRET-based genetically encoded biosensors for second messengers, protein phosphorylation and activity of small GTPases have provided insights into the spatial and temporal regulation of signaling processes [8][9][10][11][12] .The combination of enhanced cyan (CFP) and yellow (YFP) fluorescent proteins has proven to be most effective in many FRET studies. Cloning of Anthozoa fluorescent proteins, such as red DsRed 13,14 and far-red HcRed 15 , has expanded the in vivo applications of FRET, but a major limitation of Anthozoa proteins for FRET applications is their obligate oligomerization 16 . Recent generation of a monomerized mutant of DsRed, monomeric red fluorescent protein 1 (mRFP) 17 , provides the opportunity to generate functional monomeric fusion proteins and to use mRFP as a FRET acceptor with proteins fused to GFP or its mutants.Various methods of FRET measurements have been used to visualize protein-protein interactions 18 . The general limitation of these methods is that they only permit the analysis of interactions between two proteins. To analyze multi-component signaling complexes, a method to measure interactions betwe...

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Diversity and evolution of the green fluorescent protein family

Cited by 346 publications

References 32 publications

Quenching of superoxide radicals by green fluorescent protein

Quenching of superoxide radicals by green fluorescent protein

Shedding light onto live molecular targets

Three-chromophore FRET microscopy to analyze multiprotein interactions in living cells

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