Analysis of protein interactions using fluorescence technologies

Current Opinion in Chemical Biology

Volumn 7, Issue 5, 2003, Pages 635-640

  Yan, Yuling ^a   Marriott, Gerard ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHELATE; PROTEOME; SOLVENT;

ANISOTROPY; COMPLEX FORMATION; CYTOLOGY; FLUORESCENCE; HYDRODYNAMICS; IMAGING SYSTEM; MEASUREMENT; PHOTON; PROTEIN INTERACTION; QUANTUM YIELD; REVIEW; SPECTROSCOPY;

EID: 0142138241     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2003.08.017     Document Type: Review

References (32)

1. Roy P., Rajfur Z., Jones D., Marriott G., Loew L., Jacobson K. Local photorelease of caged thymosin β4 in locomoting keratocytes causes cell turning. J. Cell. Biol. 153:2001;1035-1048 In this functional proteomics study, the authors manipulated the interaction of thymosin β4 with G-actin at defined sites in a motile cell using light-directed activation of caged thymosin β4. The authors showed that the motile behavior of a cell was reproducibly perturbed by transiently increasing the level of G-actin-thymosin β4 at specific sites in the cell.
2. Zhu H., Bilgin M., Bangham R., Hall D., Casamayor A., Bertone P., Lan N., Jansen R., Bidlingmaier S., Houfek T.et al. Global analysis of protein activities using proteome chips. Science. 293:2001;2101-2105 The authors generated a spatially addressable chip harboring >90% of all yeast proteins. In one application, the proteome chip was screened with a biotin-labeled calmodulin and 33 potential calmodulin-binding proteins were identified using fluorescence detection of a Cy3-streptavidin conjugate. This study demonstrates the power of using protein chips and fluorescence-based detection for high-throughput analysis of protein interactions.
3. Truong K., Ikura M. The use of FRET imaging microscopy to detect protein-protein interactions and protein conformational changes in vivo. Curr. Opin. Struct. Biol. 11:2001;573-578.
4. Jameson D.M., Croney J.C., Moens P.D. Fluorescence: basic concepts, practical aspects, and some anecdotes. Methods Enzymol. 360:2003;1-43 An excellent and entertaining overview of fluorescence spectroscopy. The two-volume issue of Methods in Enzymology on biophotonics (Volumes 360 and 361) contains several other excellent reviews that detail state-of-the-art techniques for mapping protein interactions in vivo and in vitro.
5. Axelrod D. Total internal reflection fluorescence microscopy in cell biology. Methods Enzymol. 361:2003;1-33.
6. Hess S.T., Huang S., Heikal A.A., Webb W.W. Biological and chemical applications of fluorescence correlation spectroscopy: a review. Biochemistry. 41:2002;697-705.
7. Muller J.D., Chen Y., Gratton E. Fluorescence correlation spectroscopy. Methods Enzymol. 361:2003;69-92.
8. Centonze V.E., Sun M., Masuda A., Gerritsen H., Herman B. Fluorescence resonance energy transfer imaging microscopy. Methods Enzymol. 360:2003;542-560.
9. Clegg R.M., Holub O., Gohlke C. Fluorescence lifetime-resolved imaging: measuring lifetimes in an image. Methods Enzymol. 360:2003;509-542.
10. Marriott G, Parker I (Eds): Biophotonics. Methods Enzymol 360/361. London: Elsevier; 2003.
11. Jameson D.M., Croney J.C. Fluorescence polarization: past, present and future. Comb. Chem. High Throughput. Screen. 6:2003;167-173.
12. Clayton A.H., Hanley Q.S., Arndt-Jovin D.J., Subramaniam V., Jovin T.M. Dynamic fluorescence anisotropy imaging microscopy in the frequency domain (rFLIM). Biophys. J. 83:2002;1631-1649.
13. Fowler A., Swift D., Longman E., Acornley A., Hemsley P., Murray D., Unitt J., Dale I., Sullivan E., Coldwell M. An evaluation of fluorescence polarization and lifetime discriminated polarization for high throughput screening of serine/threonine kinases. Anal. Biochem. 308:2002;223-231.
14. Verveer P.J., Squire A., Bastiaens P.I. Improved spatial discrimination of protein reaction states in cells by global analysis and deconvolution of fluorescence lifetime imaging microscopy data. J. Microsc. 202:2001;451-456.
15. Subramaniam V., Hanley Q.S., Clayton A.H., Jovin T.M. Photophysics of green and red fluorescent proteins: implications for quantitative microscopy. Methods Enzymol. 360:2003;178-201 A goldmine of information on the photophysical properties of fluorescent proteins, with an excellent overview of experimental approaches to measure FRET.
16. Adams S.R., Campbell R.E., Gross L.A., Martin B.R., Walkup G.K., Yao Y., Llopis J., Tsien R.Y. New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications. J. Am. Chem. Soc. 124:2002;6063-6076.
17. Bastiaens P.I., Jovin T.M. Microspectroscopic imaging tracks the intracellular processing of a signal transduction protein: fluorescent-labeled protein kinase C beta I. Proc. Natl. Acad. Sci. USA. 93:1996;8407-8412.
18. Maliwal B.P., Gryczynski Z., Lakowicz J.R. Long-wavelength long-lifetime luminophores. Anal. Chem. 73:2001;4277-4285.
19. Lakowicz J.R. Radiative decay engineering: biophysical and biomedical applications. Anal. Biochem. 298:2001;1-24.
20. Erickson M.G., Alseikhan B.A., Peterson B.Z., Yue D.T. Preassociation of calmodulin with voltage-gated Ca(2+) channels revealed by FRET in single living cells. Neuron. 31:2001;973-985 An important study describing a powerful approach to quantify protein interactions based on images of FRET using CFP and YFP fusion proteins. The approach overcomes some potential problems and artifacts of using this popular donor-acceptor pair to map protein interactions within cells.
21. 2+ channel CaM preassociation. Neuron. 39:2003;97-107.
22. Bergendahl V., Heyduk T., Burgess R.R. Luminescence resonance energy transfer-based high-throughput screening assay for inhibitors of essential protein-protein interactions in bacterial RNA polymerase. Appl. Environ. Microbiol. 69:2003;1492-1498.
23. Marriott G., Clegg R.M., Arndt-Jovin D.J., Jovin T.M. Time resolved imaging microscopy-phosphorescence and delayed fluorescence imaging. Biophys. J. 60:1991;1374-1387.
24. Harpur A.G., Wouters F.S., Bastiaens P.I. Imaging FRET between spectrally similar GFP molecules in single cells. Nat. Biotechnol. 19:2001;167-169.
25. Matsumoto C., Hamasaki K., Mihara H., Ueno A. A high-throughput screening utilizing intramolecular fluorescence resonance energy transfer for the discovery of the molecules that bind HIV-1 TAR RNA specifically. Bioorg. Med. Chem. Lett. 10:2000;1857-1861.
26. Karpova T.S., Baumann C.T., He L., Wu X., Grammer A., Lipsky P., Hager G.L., McNally J.G. Fluorescence resonance energy transfer from cyan to yellow fluorescent protein detected by acceptor photobleaching using confocal microscopy and a single laser. J. Microsc. 209:2003;56-70.
27. Turconi S., Shea K., Ashman S., Fantom K., Earnshaw D.L., Bingham R.P., Haupts U.M., Brown M.J., Pope A.J. Real experiences of uHTS: a prototypic 1536-well fluorescence anisotropy-based uHTS screen and application of well-level quality control procedures. J. Biomol. Screen. 6:2001;275-290.
28. Gautier I., Tramier M., Durieux C., Coppey J., Pansu R.B., Nicolas J.C., Kemnitz K., Coppey-Moisan M. Homo-FRET microscopy in living cells to measure monomer-dimer transition of GFT-tagged proteins. Biophys J. 80:2001;3000-3008 These authors describe a general approach to quantify a monomer-dimer transition between identically labeled GFP-fusion proteins that uses microscope-based imaging of the depolarization of fluorescence emission resulting from homo-FRET between two GFP probes in the dimer. This study is important because the interaction between the monomers of the herpes simplex virus thymidine kinase is mapped using a single label, which opens up the possibility for homo-FRET-based, multiplexed analysis of protein interactions within the same cell, using protein monomers fused to specific fluorescent proteins (e.g. BFP, CFP, GFP and YFP).
29. Ventre I., Ledgham F., Prima V., Lazdunski A., Foglino M., Sturgis J.N. Dimerization of the quorum sensing regulator RhlR: development of a method using EGFP fluorescence anisotropy. Mol. Microbiol. 48:2003;187-198.
30. Yan Y., Marriott G. Fluorescence resonance energy transfer imaging microscopy and fluorescence polarization imaging microscopy. Methods Enzymol. 360:2003;561-580.
31. Patel R.C., Kumar U., Lamb D.C., Eid J.S., Rocheville M., Grant M., Rani A., Hazlett T., Patel S.C., Gratton E., Patel Y.C. Ligand binding to somatostatin receptors induces receptor-specific oligomer formation in live cells. Proc. Natl. Acad. Sci. USA. 99:2002;3294-3299.
32. Levene M.J., Korlach J., Turner S.W., Foquet M., Craighead H.G., Webb W.W. Zero-mode waveguides for single-molecule analysis at high concentrations. Science. 299:2003;682-686.