Structure-function studies on the active site of the coelenterazine- dependent luciferase from Renilla

Protein Science

Volumn 17, Issue 4, 2008, Pages 725-735

  Woo, Jongchan ^a   Howell, Matthew H ^a   Von Arnim, Albrecht G ^a  

^a UNIVERSITY OF TENNESSEE   (United States)

Author keywords

; Bioluminescence resonance energy transfer; Coelenterazine; Dioxygenase; Hydrolase

Indexed keywords

AEQUORIN; DIETHYL PYROCARBONATE; LUCIFERASE; MUTANT PROTEIN; PHOTOPROTEIN; PROTEIN INHIBITOR;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BIOLUMINESCENCE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; FLAME PHOTOMETRY; HETEROLOGOUS EXPRESSION; MOLECULAR DOCKING; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN STRUCTURE; RENILLA; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS;

AEQUORIN; AMINO ACID SEQUENCE; BINDING SITES; CATALYSIS; COMPUTER SIMULATION; DIETHYL PYROCARBONATE; IMIDAZOLES; ISOXAZOLES; LUCIFERASES, RENILLA; LUMINESCENT MEASUREMENTS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHENYLMETHYLSULFONYL FLUORIDE; PYRAZINES; STRUCTURE-ACTIVITY RELATIONSHIP;

BACTERIA (MICROORGANISMS); RENILLA; RENILLA LUCIFERASE; SPHINGOMONAS;

EID: 41649093617     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.073355508     Document Type: Article

References (33)

1. Coulon, V., Audet, M., Homburger, V., Bockaert, J., Fagni, L., Bouvier, M., and Perroy, J. 2008. Subcellular imaging of dynamic protein interactions by bioluminescence resonance energy transfer. Biophys. J. 94: 1001-1009.
2. 2+-discharged photoprotein: Implications for mechanisms of the calcium trigger and bioluminescence. J. Biol. Chem. 279: 33647-33652.
3. 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase involving general base catalysis by histidine 251 and single-electron oxidation of the substrate dianion. Biochemistry 43: 14485-14499.
4. Hart, R.C., Matthews, J.C., Hori, K., and Cormier, M.J. 1979. Renilla reniformis bioluminescence: Luciferase-catalyzed production of non-radiating excited states from luciferin analogues and elucidation of the excited state species involved in energy transfer to Renilla green fluorescent protein. Biochemistry 18: 2204-2210.
5. Head, J.F., Inouye, S., Teranishi, K., and Shimomura, O. 2000. The crystal structure of the photoprotein aequorin at 2.3 Å resolution. Nature 405: 372-376.
6. Holmquist, M. 2000. α/β-Hydrolase fold enzymes: Structures, functions and mechanisms. Curr. Protein Pept. Sci. 1: 209-235.
7. Hori, K., Wampler, J.E., Matthews, J.C., and Cormier, M.J. 1973. Identification of the product excited states during the chemiluminescent and bioluminescent oxidation of Renilla (sea pansy) luciferin and certain of its analogs. Biochemistry 12: 4463-4468.
8. Hoshino, H., Nakajima, Y., and Ohmiya, Y. 2007. Luciferase-YFP fusion tag with enhanced emission for single-cell luminescence imaging. Nat. Methods 4: 637-639.
9. Hynkova, K., Nagata, Y., Takagi, M., and Damborsky, J. 1999. Identification of the catalytic triad in the haloalkane dehalogenase from Sphingomonas paucimobilis UT26. FEBS Lett. 446: 177-181.
10. Inouye, S. and Sasaki, S. 2007. Imidazole-assisted catalysis of luminescence reaction in blue fluorescent protein from the photoprotein aequorin. Biochem. Biophys. Res. Commun. 354: 650-655.
11. 2+-regulated photoprotein obelin at 1.7 Å resolution determined directly from its sulfur substructure. Protein Sci. 9: 2085-2093.
12. 2+-triggered bioluminescence suggests neutral coelenteramide as the primary excited state. Proc. Natl. Acad. Sci. 103: 2570-2575.
13. Loening, A.M., Fenn, T.D., Wu, A.M., and Gambhir, S.S. 2006. Consensus guided mutagenesis of Renilla luciferase yields enhanced stability and light output. Protein Eng. Des. Sel. 19: 391-400.
14. Loening, A.M., Fenn, T.D., and Gambhir, S.S. 2007a. Crystal structures of the luciferase and green fluorescent protein from Renilla reniformis. J. Mol. Biol. 374: 1017-1028.
15. Loening, A.M., Wu, A.M., and Gambhir, S.S. 2007b. Red-shifted Renilla reniformis luciferase variants for imaging in living subjects. Nat. Methods 4: 641-643.
16. Mach, H., Middaugh, C.R., and Lewis, R.V. 1992. Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins. Anal. Biochem. 200: 74-80.
17. Marek, J., Vevodova, J., Smatanova, I.K., Nagata, Y., Svensson, L.A., Newman, J., Takagi, M., and Damborsky, J. 2000. Crystal structure of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26. Biochemistry 39: 14082-14086.
18. Matthews, J.C., Hori, K., and Cormier, M.J. 1977a. Purification and properties of Renilla reniformis luciferase. Biochemistry 16: 85-91.
19. Matthews, J.C., Hori, K., and Cormier, M.J. 1977b. Substrate and substrate analogue binding properties of Renilla luciferase. Biochemistry 16: 5217-5220.
20. Oakley, A.J., Klvana, M., Otyepka, M., Nagata, Y., Wilce, M.C., and Damborsky, J. 2004. Crystal structure of haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26 at 0.95 Å resolution: Dynamics of catalytic residues. Biochemistry 43: 870-878.
21. 2+-binding photoprotein, aequorin, after histidine modification. FEBS Lett. 320: 267-270.
22. Ohmiya, Y. and Hirano, T. 1996. Shining the light: The mechanism of the bioluminescence reaction of calcium-binding photoproteins. Chem. Biol. 3: 337-347.
23. Ohmiya, Y., Ohashi, M., and Tsuji, F.I. 1992. Two excited states in aequorin bioluminescence induced by tryptophan modification. FEBS Lett. 301: 197-201.
24. Schwede, T., Kopp, J., Guex, N., and Peitsch, M.C. 2003. SWISS-MODEL: An automated protein homology-modeling server. Nucleic Acids Res. 31: 3381-3385.
25. Shimomura, O. 1995. Cause of spectral variation in the luminescence of semisynthetic aequorins. Biochem. J. 306: 537-543.
26. Stepanyuk, G.A., Golz, S., Markova, S.V., Frank, L.A., Lee, J., and Vysotski, E.S. 2005. Interchange of aequorin and obelin bioluminescence color is determined by substitution of one active site residue of each photoprotein. FEBS Lett. 579: 1008-1014.
27. Streltsov, V.A., Prokop, Z., Damborsky, J., Nagata, Y., Oakley, A., and Wilce, M.C. 2003. Haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26: X-ray crystallographic studies of dehalogenation of brominated substrates. Biochemistry 42: 10104-10112.
28. Subramanian, C., Woo, J., Cai, X., Xu, X., Servick, S., Johnson, C.H., Nebenfuhr, A., and von Arnim, A.G. 2006. A suite of tools and application notes for in vivo protein interaction assays using bioluminescence resonance energy transfer (BRET). Plant J. 48: 138-152.
29. Thomsen, R. and Christensen, M.H. 2006. MolDock: A new technique for high-accuracy molecular docking. J. Med. Chem. 49: 3315-3321.
30. 2+-regulated photoproteins: Structural insight into the bioluminescence mechanism. Acc. Chem. Res. 37: 405-415.
31. Vysotski, E.S., Liu, Z.J., Markova, S.V., Blinks, J.R., Deng, L., Frank, L.A., Herko, M., Malikova, N.P., Rose, J.P., Wang, B.C., et al. 2003. Violet bioluminescence and fast kinetics from W92F obelin: Structure-based proposals for the bioluminescence triggering and the identification of the emitting species. Biochemistry 42: 6013-6024.
32. Xu, Y., Piston, D.W., and Johnson, C.H. 1999. A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins. Proc. Natl. Acad. Sci. 96: 151-156.
33. Xu, X., Soutto, M., Xie, Q., Servick, S., Subramanian, C., von Arnim, A.G., and Johnson, C.H. 2007. Imaging protein interactions with bioluminescence resonance energy transfer (BRET) in plant and mammalian cells and tissues. Proc. Natl. Acad. Sci. 104: 10264-10269.