Structural basis for the phototoxicity of the fluorescent protein KillerRed

FEBS Letters

Volumn 583, Issue 17, 2009, Pages 2839-2842

  Carpentier, Philippe ^a   Violot, Sebastien ^a   Blanchoin, Laurent ^a   Bourgeois, Dominique ^a,b  

^a CEA GRENOBLE   (France)

^b EUROPEAN SYNCHROTRON RADIATION FACILITY   (France)

Author keywords

CALI; Fluorescent proteins; Reactive oxygen species; Solvent channel; X ray crystallography

Indexed keywords

KILLERRED PROTEIN; MONOMER; PHOTOSENSITIZING AGENT; REACTIVE OXYGEN METABOLITE; RED FLUORESCENT PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BLEACHING; CHROMATOPHORE; CHROMOPHORE ASSISTED LIGHT INACTIVATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; MOLECULAR DYNAMICS; OXYGEN TRANSPORT; PHOTOTOXICITY; PRIORITY JOURNAL; PROTEIN ENGINEERING;

ANIMALS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; HYDROZOA; LIGHT; LUMINESCENT PROTEINS; MODELS, MOLECULAR; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; REACTIVE OXYGEN SPECIES;

EID: 69349092404     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.07.041     Document Type: Article

References (24)

1. Jacobson K., Rajfur Z., Vitriol E., and Hahn K. Chromophore-assisted laser inactivation in cell biology. Trends Cell Biol. 18 (2008) 443-450
2. Rajfur Z., Roy P., Otey C., Romer L., and Jacobson K. Dissecting the link between stress fibres and focal adhesions by CALI with EGFP fusion proteins. Nat. Cell Biol. 4 (2002) 286-293
3. Tanabe T., Oyamada M., Fujita K., Dai P., Tanaka H., and Takamatsu T. Multiphoton excitation-evoked chromophore-assisted laser inactivation using green fluorescent protein. Nat. Methods 2 (2005) 503-505
4. Vitriol E.A., Uetrecht A.C., Shen F., Jacobson K., and Bear J.E. Enhanced EGFP-chromophore-assisted laser inactivation using deficient cells rescued with functional EGFP-fusion proteins. Proc. Natl. Acad. Sci. USA 104 (2007) 6702-6707
5. Swaminathan R., Hoang C.P., and Verkman A.S. Photobleaching recovery and anisotropy decay of green fluorescent protein GFP-S65T in solution and cells: cytoplasmic viscosity probed by green fluorescent protein translational and rotational diffusion. Biophys. J. 72 (1997) 1900-1907
6. Horstkotte E., Schroder T., Niewohner J., Thiel E., Jay D.G., and Henning S.W. Toward understanding the mechanism of chromophore-assisted laser inactivation - evidence for the primary photochemical steps. Photochem. Photobiol. 81 (2005) 358-366
7. Jimenez-Banzo A., Nonell S., Hofkens J., and Flors C. Singlet oxygen photosensitization by EGFP and its chromophore HBDI. Biophys. J. 94 (2008) 168-172
8. Yan P., Xiong Y., Chen B., Negash S., Squier T.C., and Mayer M.U. Fluorophore-assisted light inactivation of calmodulin involves singlet-oxygen mediated cross-linking and methionine oxidation. Biochemistry 45 (2006) 4736-4748
9. Shagin D.A., et al. GFP-like proteins as ubiquitous metazoan superfamily: evolution of functional features and structural complexity. Mol. Biol. Evol. 21 (2004) 841-850
10. Bulina M.E., et al. A genetically encoded photosensitizer. Nat. Biotechnol. 24 (2006) 95-99
11. Bulina M.E., Lukyanov K.A., Britanova O.V., Onichtchouk D., Lukyanov S., and Chudakov D.M. Chromophore-assisted light inactivation (CALI) using the phototoxic fluorescent protein KillerRed. Nat. Protocols 1 (2006) 947-953
12. Gross L.A., Baird G.S., Hoffman R.C., Baldridge K.K., and Tsien R.Y. The structure of the chromophore within DsRed, a red fluorescent protein from coral. Proc. Natl. Acad. Sci. USA 97 (2000) 11990-11995
13. Baird G.S., Zacharias D.A., and Tsien R.Y. Biochemistry, mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coral. Proc. Natl. Acad. Sci. USA 97 (2000) 11984-11989
14. Evdokimov A.G., et al. Structural basis for the fast maturation of Arthropoda green fluorescent protein. EMBO Rep. 7 (2006) 1006-1012
15. Wachter R.M., Elsliger M.A., Kallio K., Hanson G.T., and Remington S.J. Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein. Structure 6 (1998) 1267-1277
16. Nienhaus K., Renzi F., Vallone B., Wiedenmann J., and Nienhaus G.U. Exploring chromophore-protein interactions in fluorescent protein cmFP512 from Cerianthus membranaceus: X-ray structure analysis and optical spectroscopy. Biochemistry 45 (2006) 12942-12953
17. Adam, V., Carpentier, P., Violot, S., Lelimousin, M., Darnault, C., Nienhaus, G.U. and Bourgeois, D. (submitted for publication).
18. Serebrovskaya E.O., Edelweiss E.F., Stremovskiy O.A., Lukyanov K.A., Chudakov D.M., and Deyev S.M. Targeting cancer cells by using an antireceptor antibody-photosensitizer fusion protein. Proc. Natl. Acad. Sci. USA 106 (2009) 9221-9225
19. Hoogenboom J.P., van Dijk E.M., Hernando J., van Hulst N.F., and Garcia-Parajo M.F. Power-law-distributed dark states are the main pathway for photobleaching of single organic molecules. Phys. Rev. Lett. 95 (2005) 097401
20. Zondervan R., Kulzer F., Kol'chenko M.A., and Orrit M. Photobleaching of rhodamine 6G in poly(vinyl alcohol) at the ensemble and single-molecule levels. J. Phys. Chem. A 108 (2004) 1657-1665
21. Bogdanov A.M., et al. Green fluorescent proteins are light-induced electron donors. Nat. Chem. Biol. 5 (2009) 459-461
22. Luo S., and Levine R.L. Methionine in proteins defends against oxidative stress. FASEB J. 23 (2009) 464-472
23. Bell A.F., Stoner-Ma D., Wachter R.M., and Tonge P.J. Light-driven decarboxylation of wild-type green fluorescent protein. J. Am. Chem. Soc. 125 (2003) 6919-6926
24. van Thor J.J., Gensch T., Hellingwerf K.J., and Johnson L.N. Phototransformation of green fluorescent protein with UV and visible light leads to decarboxylation of glutamate 222. Nat. Struct. Biol. 9 (2002) 37-41