Nontrivial Effect of the Color-Exchange of a Donor/Acceptor Pair in the Engineering of Förster Resonance Energy Transfer (FRET)-Based Indicators

ACS Chemical Biology

Volumn 11, Issue 7, 2016, Pages 1816-1822

  Ohta, Yusaku ^a   Kamagata, Takanori ^a,b,c   Mukai, Asuka ^a   Takada, Shinji ^b,c   Nagai, Takeharu ^d   Horikawa, Kazuki ^a  

^a UNIVERSITY OF TOKUSHIMA   (Japan)

^b OKAZAKI INSTITUTE FOR INTEGRATIVE BIOSCIENCE   (Japan)

^c GRADUATE UNIVERSITY FOR ADVANCED STUDIES   (Japan)

^d OSAKA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CIRCULARLY PERMUTED FLUORESCENT PROTEIN; CYCLIC AMP; CYCLIC GMP; CYCLIC GMP DEPENDENT PROTEIN KINASE 1; FLUORESCENT DYE; UNCLASSIFIED DRUG;

ARTICLE; BIOCHEMICAL ANALYSIS; COLOR; COMPARATIVE STUDY; CONTROLLED STUDY; DICTYOSTELIUM DISCOIDEUM; ENERGY TRANSFER; EXTRACELLULAR SPACE; FLUORESCENCE RESONANCE ENERGY TRANSFER; HEK293 CELL LINE; NONHUMAN; PRIORITY JOURNAL; CHEMISTRY; PROCEDURES;

COLOR; FLUORESCENCE RESONANCE ENERGY TRANSFER; FLUORESCENT DYES;

EID: 84978657053     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.6b00221     Document Type: Article

References (29)

1. Jares-Erijman, E. A. and Jovin, T. M. (2003) FRET imaging Nat. Biotechnol. 21, 1387-1395 10.1038/nbt896
2. 2+based on green fluorescent proteins and calmodulin Nature 388, 882-887 10.1038/42264
3. Miyawaki, A. and Niino, Y. (2015) Molecular Spies for Bioimaging-Fluorescent Protein-Based Probes Mol. Cell 58, 632-643 10.1016/j.molcel.2015.03.002
4. Lindenburg, L. and Merkx, M. (2014) Engineering Genetically Encoded FRET Sensors Sensors 14, 11691-11713 10.3390/s140711691
5. Lakowicz, J. R. (2006) Principles of Fluorescence Spectroscopy, Springer US, Boston, MA.
6. Xue, L., Prifti, E., and Johnsson, K. (2016) A General Strategy for the Semisynthesis of Ratiometric Fluorescent Sensor Proteins with Increased Dynamic Range J. Am. Chem. Soc. 138, 5258-5261 10.1021/jacs.6b03034
7. O'Hare, H. M., Johnsson, K., and Gautier, A. (2007) Chemical probes shed light on protein function Curr. Opin. Struct. Biol. 17, 488-494 10.1016/j.sbi.2007.07.005
8. Nagai, T. and Miyawaki, A. (2004) A high-throughput method for development of FRET-based indicators for proteolysis Biochem. Biophys. Res. Commun. 319, 72-77 10.1016/j.bbrc.2004.04.147
9. Komatsu, N., Aoki, K., Yamada, M., Yukinaga, H., Fujita, Y., Kamioka, Y., and Matsuda, M. (2011) Development of an optimized backbone of FRET biosensors for kinases and GTPases Mol. Biol. Cell 22, 4647-4656 10.1091/mbc.E11-01-0072
10. Kotera, I., Iwasaki, T., Imamura, H., Noji, H., and Nagai, T. (2010) Reversible Dimerization of Aequorea victoria Fluorescent Proteins Increases the Dynamic Range of FRET-Based Indicators ACS Chem. Biol. 5, 215-222 10.1021/cb900263z
11. Nguyen, A. W. and Daugherty, P. S. (2005) Evolutionary optimization of fluorescent proteins for intracellular FRET Nat. Biotechnol. 23, 355-360 10.1038/nbt1066
12. Vinkenborg, J. L., Evers, T. H., Reulen, S. W. A., Meijer, E. W., and Merkx, M. (2007) Enhanced Sensitivity of FRET-Based Protease Sensors by Redesign of the GFP Dimerization Interface ChemBioChem 8, 1119-1121 10.1002/cbic.200700109
13. 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. U. S. A. 101, 10554-10559 10.1073/pnas.0400417101
14. Mizutani, T., Kondo, T., Darmanin, S., Tsuda, M., Tanaka, S., Tobiume, M., Asaka, M., and Ohba, Y. (2010) A Novel FRET-Based Biosensor for the Measurement of BCR-ABL Activity and Its Response to Drugs in Living Cells Clin. Cancer Res. 16, 3964-3975 10.1158/1078-0432.CCR-10-0548
15. Allen, M. D. and Zhang, J. (2006) Subcellular dynamics of protein kinase A activity visualized by FRET-based reporters Biochem. Biophys. Res. Commun. 348, 716-721 10.1016/j.bbrc.2006.07.136
16. Fritz, R. D., Letzelter, M., Reimann, A., Martin, K., Fusco, L., Ritsma, L., Ponsioen, B., Fluri, E., Schulte-Merker, S., van Rheenen, J., and Pertz, O. (2013) A Versatile Toolkit to Produce Sensitive FRET Biosensors to Visualize Signaling in Time and Space Sci. Signaling 6, rs12 10.1126/scisignal.2004135
17. Piljić, A., de Diego, I., Wilmanns, M., and Schultz, C. (2011) Rapid Development of Genetically Encoded FRET Reporters ACS Chem. Biol. 6, 685-691 10.1021/cb100402n
18. Rekas, A., Alattia, J.-R., Nagai, T., Miyawaki, A., and Ikura, M. (2002) Crystal Structure of Venus, a Yellow Fluorescent Protein with Improved Maturation and Reduced Environmental Sensitivity J. Biol. Chem. 277, 50573-50578 10.1074/jbc.M209524200
19. Lelimousin, M., Noirclerc-Savoye, M., Lazareno-Saez, C., Paetzold, B., Le Vot, S., Chazal, R., Macheboeuf, P., Field, M. J., Bourgeois, D., and Royant, A. (2009) Intrinsic Dynamics in ECFP and Cerulean Control Fluorescence Quantum Yield Biochemistry 48, 10038-10046 10.1021/bi901093w
20. Nikolaev, V. O., Gambaryan, S., and Lohse, M. J. (2006) Fluorescent sensors for rapid monitoring of intracellular cGMP Nat. Methods 3, 23-25 10.1038/nmeth816
21. Russwurm, M., Mullershausen, F., Friebe, A., Jager, R., Russwurm, C., and Koesling, D. (2007) Design of fluorescence resonance energy transfer (FRET)-based cGMP indicators: a systematic approach Biochem. J. 407, 69-77 10.1042/BJ20070348
22. Honda, A., Adams, S. R., Sawyer, C. L., Lev-Ram, V., Tsien, R. Y., and Dostmann, W. R. G. (2001) Spatiotemporal dynamics of guanosine 3′,5′-cyclic monophosphate revealed by a genetically encoded, fluorescent indicator Proc. Natl. Acad. Sci. U. S. A. 98, 2437-2442 10.1073/pnas.051631298
23. Reed, R. B., Sandberg, M., Jahnsen, T., Lohmann, S. M., Francis, S. H., and Corbin, J. D. (1996) Fast and Slow Cyclic Nucleotide-dissociation Sites in cAMP-dependent Protein Kinase Are Transposed in Type Iβ cGMP-dependent Protein Kinase J. Biol. Chem. 271, 17570-17575 10.1074/jbc.271.29.17570
24. Mato, J. M., Van Haastert, P. J. M., Krens, F. A., Rhunsburger, E. H., Dobbe, F. C. P. M., and Konijn, T. M. (1977) Cyclic AMP and folic acid mediated cyclic GMP accumulation in Dictyostelium discoideum FEBS Lett. 79, 331-336 10.1016/0014-5793(77)80814-4
25. Gerisch, G., Malchow, D., Roos, W., and Wick, U. (1979) Oscillations of cyclic nucleotide concentrations in relation to the excitability of Dictyostelium cells J. Exp. Biol. 81, 33-47
26. Fisher, P. R., Merkl, R., and Gerisch, G. (1989) Quantitative analysis of cell motility and chemotaxis in Dictyostelium discoideum by using an image processing system and a novel chemotaxis chamber providing stationary chemical gradients J. Cell Biol. 108, 973-984 10.1083/jcb.108.3.973
27. Herberg, F. W., Dostmann, W. R. G., Zorn, M., Davis, S. J., and Taylor, S. S. (1994) Crosstalk between Domains in the Regulatory Subunit of cAMP-Dependent Protein Kinase: Influence of Amino Terminus on cAMP Binding and Holoenzyme Formation Biochemistry 33, 7485-7494 10.1021/bi00189a057
28. Ibraheem, A., Yap, H., Ding, Y., and Campbell, R. E. (2011) A bacteria colony-based screen for optimal linker combinations in genetically encoded biosensors BMC Biotechnol. 11, 105 10.1186/1472-6750-11-105
29. Hires, S. A., Zhu, Y., and Tsien, R. Y. (2008) Optical measurement of synaptic glutamate spillover and reuptake by linker optimized glutamate-sensitive fluorescent reporters Proc. Natl. Acad. Sci. U. S. A. 105, 4411-4416 10.1073/pnas.0712008105