Yellow fluorescent proteins

Two types of fluorescent proteins have been isolated from luminous bacteria and studied in detail. The first of them are the blue fluorescent lumazine proteins (LumPs) containing lumazine as their chromophores, which were isolated from P. phosphoreum and P. fischeri (Gast and Lee, 1978 Koda and Lee, 1979 O Kane et al.y 1985). The second are the yellow fluorescent proteins (YFPs) containing a chromophore of FMN or riboflavin, isolated from P. fischeri strain Y-l (Daubner et al., 1987 Macheroux et ai, 1987 ... 

Daubner, S. C., and Baldwin, T. O. (1989). Interaction between luciferase from various species of bioluminescent bacteria and the Yellow Fluorescent Protein of Vibrio fischeri strain Y-l. Biochem. Biophys. Res. Commun. 161 1191-1198. 

Daubner, S. C., Astorga, A. M., Leisman, G. B., and Balwin, T. O. (1987). Yellow light emission of Vibrio barveyi strain Y-l purification and characterization of the energy-accepting yellow fluorescent protein. Proc. Natl. Acad. Sci. USA 84 8912-8916. 

Karatani, H., and Hastings, J. W. (1993). Two active forms of the accessory yellow fluorescence protein of the luminous bacterium Vibrio fischeri strain Yl. J. Photochem. Photobiol., B 18 227-232. 

Macheroux, P., et al. (1987). Purification of the yellow fluorescent protein from Vibrio fischeri and identity of the flavin chromophore. Biochem. Biophys. Res. Commun. 146 101-106. 

Visser, A. J. W. G., et al. (1997). Time-dissolved fluorescence study of the dissociation of FMN from the yellow fluorescence protein from Vibrio fischeri. Photochem. Photobiol. 65 570-575. 

Borst JW, Flink MA, van Hoek A, Visser AJWG (2005) Effects of refractive index and viscosity on fluorescence and anisotropy decays of enhanced cyan and yellow fluorescent proteins. JFluoresc 15 153-160... 

Schwille P, Kummer S, Heikal AA, Moemer WE, Webb WW (2000) Fluorescence correlation spectroscopy reveals fast optical excitation-driven intramolecular dynamics of yellow fluorescent proteins. Proc Natl Acad Sci USA 97 151-156... 

Shi X, Basran J, Seward FIE, Childs W, Bagshaw CR, Boxer SG (2007) Anomalous negative fluorescence anisotropy in yellow fluorescent protein (YFP 10C) quantitative analysis of FRET in YFP dimers. Biochemistry 46 14403-14417... 

McAnaney TB, Zeng W, Doe CFE, Bhanji N, Wakelin S, Pearson DS, Abbyad P, Shi XH, Boxer SG, Bagshaw CR (2005) Protonation, photobleaching, and photoactivation of yellow fluorescent protein (YFP 10C) a unifying mechanism. Biochemistry 44 5510-5524... 

Remington SJ, Wachter RM, Yarbrough DK, Branchaud B, Anderson DC, Kallio K, Lukyanov KA (2005) zFP538, a yellow-fluorescent protein from Zoanthus, contains a novel three-ring chromophore. Biochemistry 44 202-212... 

Shaner NC, Campbell RE, Steinbach PA, Giepmans BN, Palmer AE, Tsien RY (2004) Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat Biotechnol 22 1567-1572... 

Nagai, T., Yamada, S., Tominaga, T., Ichikawa, M. and Miyawaki, A. (2004). Expanded dynamic range of fluorescent indicators for Ca2+ by circularly permuted yellow fluorescent proteins. Proc. Natl. Acad. Sci. USA 101, 10554-9. 

Cyan fluorescent proteins (CFPs) have blue-shifted excitation and emission spectra, because of the mutation Tyr66Trp inside the chromophore (Fig. 5.3C) [34], CFP fluorescence (Ex 435 nm/Em 474 nm) is less blue-shifted than for EBFP and CFP excitation is intermediate to the excitation of the neutral and anionic chromo-phores of avGFP [4], CFPs are widely used for dual-color imaging and FRET applications together with yellow fluorescent proteins (YFP, Section 3.6). 

Nagai, T., Ibata, K., Park, E. S., Kubota, M., Mikoshiba, K. and Miyawaki, A. (2002). A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 

Ganesan, S., Ameer-Beg, S. M., Ng, T. T., Vojnovic, B. and Wouters, F. S. (2006). A dark yellow fluorescent protein (YFP)-based Resonance Energy-Accepting Chromoprotein (REACh) for Forster resonance energy transfer with GFP. Proc. Natl. Acad. Sci. USA 103, 4089-94. 

Shimozono, S., Hosoi, H., Mizuno, H., Fukano, T., Tahara, T. and Miyawaki, A. (2006). Concatenation of cyan and yellow fluorescent proteins for efficient resonance energy transfer. Biochemistry 45, 6267-71. 

Rizzo, M. A., Springer, G., Segawa, K., Zipfel, W. R. and Piston, D. W. (2006). Optimization of pairings and detection conditions for measurment of FRET between cyan and yellow fluorescent proteins. Microsc. Micro-anal. 12, 238-54. 

Karpova, T. S., Baumann, C. T., He, L., Wu, X., Grammer, A., Lipsky, P., Hager, G. L. and McNally, J. G. (2003). Fluorescence resonance energy transfer from cyan to yellow fluorescent protein detected by acceptor photobleaching using confocal microscopy and a single laser. J. Microsc. 209, 56-70. 

UV VC A VE YFP Ultraviolet Virus capsid antigens Vitamin E Yellow fluorescent protein... 

Similarly to dyes, some fluorescent proteins can be incorporated into polymeric beads to be used as an alternative for ion sensing. For example, a reporter protein (composed of a phosphate-binding protein, a FRET donor (cyan fluorescent protein) and a FRET acceptor (yellow fluorescent protein)) was incorporated into polyacrylamide nanobeads by Sun et al. [46]. FRET was inhibited upon binding of phosphate. Kopelman and co-workers [47] used a similar approach to design a nanosensor for copper ions. They have found that fluorescence of red fluorescent protein DsRed (commonly used as a label) is reversibly quenched by Cu2+ and Cu+. Both DsRed and Alexa Fluor 488 (used as a reference) were entrapped into polyacrylamide nanobeads. Typically, up to 2 ppb of copper ions can be reliably measured. It should be mentioned, that in contrast to much more robust dyes, mild conditions upon polymerization and purification are very important for immobilization of the biomolecule to avoid degradation. 

FRET requires the presence of two fluorophores, one with a shorter emission wavelength (donor) and another with a longer emission wavelength (acceptor). The fluorophores must be chosen such that there is sufficient overlap of the donor emission spectrum and the acceptor excitation spectrum. When FRET occurs, which requires the proximity of the two fluorophores, excitation of the donor results in transfer of energy to the acceptor and, hence, emission at the wavelength characteristic for the acceptor. FRET can be seen with various kinds of fluorophores, but most recendy it has been used in particular with variants of GFPs because this permits FRET in intact cells. The most frequently used pairs of GFPs are the cyan fluorescent protein (CFP) and the yellow fluorescent protein (YFP) variants. The donor CFP is excited at its maximum... 

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