Abstract
Fluorescent proteins provide the opportunity to glimpse inside a living cell and obtain useful biochemical information pertaining to a variety of biological systems. These probes are unique when compared with synthetic fluorophores since they are genetically encoded and can be expressed and retained within the living cell. And, importantly, fluorescent protein fusions have enabled investigation of intracellular transport and localization of various proteins [1–3]. While fluorescent proteins are already ubiquitous in biological research, they are set to become key tools for intracellular sensing, reversible protein interaction screening, and protein engineering.
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References
J. Hahn, B. Maier, B. J. Haijema, M. Sheetz and D. Dubnau, Transformation proteins and DNA uptake localize to the cell poles in bacillus subtilis, Cell 122(1), 59–71 (2005).
K. Muntener, R. Zwicky, G. Csucs, J. Rohrer and A. Baici, Exon skipping of cathepsin B: mitochondrial targeting of a lysosomal peptidase provokes cell death, J Biol Chem 279(39), 41012–41017 (2004).
I. Vandenbroucke, P. Van Oostveldt, E. Coene, A. De Paepe and L. Messiaen, Neurofibromin is actively transported to the nucleus, FEBS Lett 560(1–3), 98–102 (2004).
L. Stryer and R. P. Haugland, Energy transfer: a spectroscopic ruler, Proc Natl Acad Sci U S A 58(2), 719–726 (1967).
T. Forster, Zwischenmolekulare Energiewanderung und Fluoreszenz, Ann Phys 2(1–2), 55–75 (1948).
B. W. Van Der Meer, G. Coker and S. Y. S. Chen, Resonance Energy Transfer Theory and Data (VCH Publishers Inc, New York, 1994).
R. Y. Tsien, The green fluorescent protein, Annu Rev Biochem 67, 509–544 (1998).
S. Karasawa, T. Araki, T. Nagai, H. Mizuno and A. Miyawaki, Cyan-emitting and orange-emitting fluorescent proteins as a donor/acceptor pair for fluorescence resonance energy transfer, Biochem J 381(Pt 1), 307–312 (2004).
G. H. Patterson, D. W. Piston and B. G. Barisas, Forster distances between green fluorescent protein pairs, Anal Biochem 284(2), 438–440 (2000).
M. Fehr, W. B. Frommer and S. Lalonde, Visualization of maltose uptake in living yeast cells by fluorescent nanosensors, Proc Natl Acad Sci U S A 99(15), 9846–9851 (2002).
M. Fehr, S. Lalonde, I. Lager, M. W. Wolff and W. B. Frommer, In vivo imaging of the dynamics of glucose uptake in the cytosol of COS-7 cells by fluorescent nanosensors, J Biol Chem 278(21), 19127–19133 (2003).
M. A. Dwyer and H. W. Hellinga, Periplasmic binding proteins: a versatile superfamily for protein engineering, Curr Opin Struct Biol 14(4), 495–504 (2004).
A. Miyawaki, J. Llopis, R. Heim, J. M. McCaffery, J. A. Adams, M. Ikura and R. Y. Tsien, Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin, Nature 388(6645), 882–887 (1997).
B. A. Pollok and R. Heim, Using GFP in FRET-based applications, Trends Cell Biol 9(2), 57–60 (1999).
H. Mizuno, A. Sawano, P. Eli, H. Hama and A. Miyawaki, Red fluorescent protein from Discosoma as a fusion tag and a partner for fluorescence resonance energy transfer, Biochemistry 40(8), 2502–2510 (2001).
O. Griesbeck, G. S. Baird, R. E. Campbell, D. A. Zacharias and R. Y. Tsien, Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications, J Biol Chem 276(31), 29188–29194 (2001).
N. Billinton and A. W. Knight, Seeing the wood through the trees: a review of techniques for distinguishing green fluorescent protein from endogenous autofluorescence, Anal Biochem 291(2), 175–197 (2001).
R. Y. Tsien, Rosy dawn for fluorescent proteins, Nat Biotechnol 17(10), 956–957 (1999).
G. S. Baird, D. A. Zacharias and R. Y. Tsien, Biochemistry, mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coral, Proc Natl Acad Sci U S A 97(22), 11984–11989 (2000).
M. A. Rizzo, G. H. Springer, B. Granada and D. W. Piston, An improved cyan fluorescent protein variant useful for FRET, Nat Biotechnol 22(4), 445–449 (2004).
T. Nagai, K. Ibata, E. S. Park, M. Kubota, K. Mikoshiba and A. Miyawaki, A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications, Nat Biotechnol 20(1), 87–90 (2002).
J. E. Bader and A. G. Beck-Sickinger, Fluorescence resonance energy transfer to study receptor dimerization in living cells, Methods Mol Biol 259, 335–352 (2004).
Q. Xu, W. J. Brecht, K. H. Weisgraber, R. W. Mahley and Y. Huang, Apolipoprotein E4 domain interaction occurs in living neuronal cells as determined by fluorescence resonance energy transfer, J Biol Chem 279(24), 25511–25516 (2004).
P. Tawa, J. Tam, R. Cassady, D. W. Nicholson and S. Xanthoudakis, Quantitative analysis of fluorescent caspase substrate cleavage in intact cells and identification of novel inhibitors of apoptosis, Cell Death Differ 8(1), 30–37 (2001).
B. P. Cormack, R. H. Valdivia and S. Falkow, FACS-optimized mutants of the green fluorescent protein (GFP), Gene 173(1 Spec No), 33–38 (1996).
R. E. Campbell, O. Tour, A. E. Palmer, P. A. Steinbach, G. S. Baird, D. A. Zacharias and R. Y. Tsien, A monomeric red fluorescent protein, Proc Natl Acad Sci U S A 99(12), 7877–7882 (2002).
N. C. Shaner, R. E. Campbell, P. A. Steinbach, B. N. Giepmans, A. E. Palmer and R. Y. Tsien, Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein, Nat Biotechnol 22(12), 1567–1572 (2004).
V. V. Verkhusha and K. A. Lukyanov, The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins, Nat Biotechnol 22(3), 289–296 (2004).
A. W. Nguyen and P. S. Daugherty, Evolutionary optimization of fluorescent proteins for intracellular FRET, Nat Biotechnol 23(3), 355–360 (2005).
T. Nagai and A. Miyawaki, A high-throughput method for development of FRET-based indicators for proteolysis, Biochem Biophys Res Commun 319(1), 72–77 (2004).
S. Fields and R. Sternglanz, The two-hybrid system: an assay for protein-protein interactions, Trends Genet 10(8), 286–292 (1994).
G. Georgiou, Analysis of large libraries of protein mutants using flow cytometry, Adv Prot Chem 55, 293–315 (2000).
K. Bernath, M. Hai, E. Mastrobattista, A. D. Griffiths, S. Magdassi and D. S. Tawfik, In vitro compartmentalization by double emulsions: sorting and gene enrichment by fluorescence activated cell sorting, Anal Biochem 325(1), 151–157 (2004).
J. Jones, R. Heim, E. Hare, J. Stack and B. A. Pollok, Development and application of a GFP-FRET intracellular caspase assay for drug screening, J Biomol Screen 5(5), 307–318 (2000).
E. T. Boder and K. D. Wittrup, Optimal screening of surface-displayed polypeptide libraries, Biotechnol Prog 14(1), 55–62 (1998).
C. Oefner, A. D'Arcy, M. Hennig, F. K. Winkler and G. E. Dale, Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon, J Mol Biol 296(2), 341–349 (2000).
B. R. Harvey, G. Georgiou, A. Hayhurst, K. J. Jeong, B. L. Iverson and G. K. Rogers, Anchored periplasmic expression, a versatile technology for the isolation of high-affinity antibodies from Escherichia coli-expressed libraries, Proc Natl Acad Sci U S A 101(25), 9193–9198 (2004).
M. T. Madigan, J. M. Martinko and J. Parker, Brock’s Biology of Microorganisms, 9th Edition (Prentice Hall, Englewood Cliffs, NJ, 2000).
L. He, X. Wu, J. Simone, D. Hewgill and P. E. Lipsky, Determination of tumor necrosis factor receptor-associated factor trimerization in living cells by CFP->YFP->mRFP FRET detected by flow cytometry, Nucleic Acids Res 33 (6), e61 (2005).
M. A. Rizzo and D. W. Piston, High-contrast imaging of fluorescent protein FRET by fluorescence polarization microscopy, Biophys J 88(2), L14–L16 (2005).
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Nguyen, A.W., You, X., Jabaiah, A.M., Daugherty, P.S. (2010). Fluorescent Protein FRET Applications. In: Geddes, C.D. (eds) Reviews in Fluorescence 2008. Reviews in Fluorescence 2008, vol 2008. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-1260-2_13
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DOI: https://doi.org/10.1007/978-1-4419-1260-2_13
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