NMR analysis of the Mg2+-binding properties of aequorin, a Ca2+-binding photoprotein

Journal of Biochemistry

Volumn 138, Issue 5, 2005, Pages 613-620

  Ohashi, Wakana ^a   Inouye, Satoshi ^b   Yamazaki, Toshio ^a   Hirota, Hiroshi ^a  

^a RIKEN YOKOHAMA INSTITUTE   (Japan)

^b CHISSO CORPORATION   (Japan)

Author keywords

Bioluminescence; EF hand; Magnesium; NMR; Photoprotein

Indexed keywords

AEQUORIN; CALCIUM; MAGNESIUM ION; MONOMER; PHOTOPROTEIN; CALCIUM BINDING PROTEIN; MAGNESIUM;

ARTICLE; BINDING AFFINITY; BINDING SITE; BIOLUMINESCENCE; CONFORMATIONAL TRANSITION; LIGHT; METAL BINDING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN AGGREGATION; PROTEIN FAMILY; PROTEIN MOTIF; PROTEIN STABILITY; PROTEIN STRUCTURE; TITRIMETRY; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; PROTEIN BINDING; PROTEIN CONFORMATION;

AEQUORIN; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CALCIUM-BINDING PROTEINS; LUMINESCENT PROTEINS; MAGNESIUM; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION;

EID: 30344478234     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvi164     Document Type: Article

References (41)

1. Shimomura, O., Johnson, F.H., and Saiga, Y. (1962) Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan. Aequorea. J. Cell. Comp. Physiol. 59, 223-240
2. Shimomura, O. and Johnson, F.H. (1979) Chemistry of the calcium-sensitive photoprotein aequorin. In Detection and Measurement of Free Calcium Ions in Cells (Ashley, C.C. and Campbell, A.K., eds.) pp. 73-83, Elsevier, North Amsterdam
3. Shimomura, O. (1983) Bioluminescence. Photochem. Photobiol. 38, 773-779
4. Shimomura, O. and Johnson, F.H. (1976) Calcium-triggered luminescence of the photoprotein aequorin. Symp. Soc. Exptl. Biol. 30, 41-54
5. Blinks, J.R., Prendergast, F.G., and Allen, D.G. (1976) Photoproteins as biological calcium indicators. Pharmacol. Rev. 28, 1-93
6. Blinks, J.R. (1985) In Bioluminescence and Chemiluminescence: Instrumental Applications (K. Van Dyke, ed.) Vol. 2. pp. 185-226, CRC, Boca Raton, FL
7. Shimomura, O. and Johnson, F.H. (1978) Peroxidized coelenterazine, the active group in the photoprotein aequorin. Proc. Natl. Acad. Sci. USA 75, 2611-2615
8. 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
9. Inouye, S., Noguchi, M., Sakaki, Y., Takagi, Y., Miyata, T., Iwanaga, S. Miyata, T., and Tsuji, F.I. (1985) Cloning and sequence analysis of cDNA for the luminescent protein aequorin. Proc. Natl. Acad. Sci. USA 82, 3154-3158
10. Charbonneau, H., Walsh, A.K., McCann, R.O., Prendergast, F.G., Cormier, M.J., and Vanaman, T.C. (1985) Amino acid sequence of the calcium-dependent photoprotein aequorin. Biochemistry 24, 6762-6771
11. Kretsinger, R.H. and Nockolds, C.E. (1973) Carp muscle calcium-binding protein. II. Structure determination and general description. J. Biol. Chem. 248, 3313-3326
12. Kawasaki, H., Nakayama, S., and Kretsinger, R.H. (1998) Classification and evolution of EF-hand proteins. Biometals 4, 277-295
13. Shimomura, O. (1995) Luminescence of aequorin is triggered by the binding of two calcium ions. Biochem. Biophys. Res. Commun. 211, 359-363
14. Shimomura, O. and Inouye, S. (1996) Titration of recombinant aequorin with calcium chloride. Biochem. Biophys. Res. Commun. 221, 77-81
15. Izutsu, K.T., Felton, S.P., Siegel, I.A., Yoda, W.T., and Chen, A.C.N. (1972) Aequorin: its ionic specificity. Biochem. Biophys. Res. Commun. 49, 1034-1039
16. Shimomura, O. and Johnson, F.H. (1973) Further data on the specificity of aequorin luminescence to calcium. Biochem. Biophys. Res. Commun. 53, 490-494
17. Allen, D.G., Blinks, J.R., and Prendergast, F.G. (1977) Aequorin luminescence: relation of light emission to calcium concentration - a calcium-independent component. Science 196, 996-998
18. Ray, B.C., Ho, S., Kemple, M.D., Prendergast, F.G., and Nageswara Rao, B.D.N. (1985) Proton NMR of aequorin. Structural changes concomitant with calcium-independent light emission. Biochemistry 24, 4280-4287
19. Moisecu, D.G., Ashley, C.C., and Campbell, A.K. (1975) Comparative aspects of the calcium-sensitive photoproteins aequorin and obelin. Biochim. Biophys. Acta 369, 133-140
20. Illarionov, B.A., Frank, L.A., Illarionova, V.A., Bondar, V.S., Vysotski, E.S., and Blinks, J.R. (2000) Recombinant obelin: Cloning and expression of cDNA, purification, and characterization as a calcium indicator. Methods Enzymol. 305, 223-249
21. Moisescu, D.G. and Ashley, C.C. (1977) The effect of physiologically occurring cations upon aequorin light emission. Determination of the binding constants. Biochim. Biophys. Acta 460, 189-205
22. Hastings, J.W., Mitchell, G., Mattingly, P.H., Blinks, J.R., and van Leeuwen, M. (1969) Response of aequorin bioluminescence to rapid changes in calcium concentration. Nature 222, 1047-1050
23. Potter, J.F. and Gergely, J. (1975) The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase. J. Biol. Chem. 250, 4628-4633
24. 2+-binding photoprotein aequorin. J. Biomol. NMR 31, 375-376
25. Inoue, S., Sugiura, S., Kakoi, H., Hasuzume, K., Goto, T., and Iio, H. (1975) Squid bioluminescence II. Isolation from Watasenia scintillans and synthesis of 2-(p-hydroxybenzyl)-6-(p-hydroxyphenyl)-3,7-dihydroimidazo[1,2- α]pyrazin-3-one. Chem. Lett. 141-144
26. 2+-binding protein, apoaequorin. J. Biochem. 105, 473-477
27. Inouye, S., Zenno, S., Sakaki, Y., and Tsuji, F.I. (1991) High-level expression and purification of apoaequorin. Protein Expres. Purif. 2, 122-126
28. Shimomura, O. and Inouye, S. (1999) The in situ regeneration and extraction of recombinant aequorin from Escherichia coli cells and the purification of extracted aequorin. Protein Expres. Purif. 16, 91-95
29. Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293
30. Johnson, B. and Blevins, R. (1994) NMRView: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4, 603-614
31. Ikura, M., Minowa, O., Yazawa, M., Yagi, K., and Hikichi, K. (1987) Sequence-specific assignments of downfield-shifted amide proton resonances of calmodulin. FEBS Lett. 219, 17-21
32. Spyracopoulos, L., Li, M.X., Sia, S.K., Gagne, S.M., Chandra, M., Solaro, R.J., and Sykes, B.D. (1997) Calcium-induced structural transition in the regulatory domain of human cardiac troponin C. Biochemistry 36, 12138-12146
33. Zhang, M., Tanaka, T., and Ikura, M. (1995) Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nat. Struct. Biol. 2, 758-767
34. 2+-activated photoprotein aequorin with reduced affinity for calcium. Biochem. Biophys. Res. Commun. 187, 1091-1097
35. Allen, D.G. and Blinks, J.R. (1978) Calcium transients in aequorin-injected frog cardiac muscle. Nature 273, 509-513
36. 2+ binding sites of troponin C in the regulation of skeletal muscle contraction. J. Biol. Chem. 271, 8381-8386
37. 2+ sites on troponin C in the regulation of muscle contraction. Preparation and properties of troponin C depleted myofibrils. J. Biol. Chem. 257, 7678-7683
38. Toma, S., Chong, K.T., Nakagawa, A., Teranishi, K., Inouye, S., and Shimomura, O. (2005) The crystal structures of semi-synthetic aequorins. Protein Sci. 14, 409-416
39. Oishi, O., Nagatomo, A., Kohzuma, T., Oda, N., Miyazima, T., Ohno, M., and Sakaki, Y. (1992) Validity of putative calcium binding loops of photoprotein aequorin. FEBS Lett. 307, 272-274
40. 2+-loaded structure. Biochemistry 43, 11371-11379
41. 2+ on target recognition by calmodulin. Biochemistry 36, 4309-4316