Tuning the affinity for lanthanides of calcium binding proteins

Biochemistry

Volumn 42, Issue 26, 2003, Pages 8011-8021

  Bertini, Ivano ^a   Gelis, Ioannis ^b   Katsaros, Nikolaos ^b   Luchinat, Claudio ^a   Provenzani, Alessandro ^a  

^a UNIVERSITY OF FLORENCE   (Italy)

^b INSTITUTE OF NANOSCIENCE AND NANOTECHNOLOGY   (Greece)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; DERIVATIVES; PROTEINS; RARE EARTH ELEMENTS;

INTERDOMAIN LINKER;

BIOCHEMISTRY;

CALCIUM; CALCIUM BINDING PROTEIN; CALMODULIN; DYSPROSIUM; LANTHANIDE; MUTANT PROTEIN; NITROGEN 15; TERBIUM; THULIUM; YTTERBIUM;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; METAL BINDING; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTON NUCLEAR MAGNETIC RESONANCE; TITRIMETRY; VERTEBRATE;

ANIMALS; BINDING SITES; CALCIUM; CALMODULIN; EF HAND MOTIFS; LANTHANOID SERIES ELEMENTS; MUTAGENESIS, SITE-DIRECTED; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; THERMODYNAMICS;

VERTEBRATA;

EID: 0038723707     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi034494z     Document Type: Article

References (55)

1. Kawasaki, K., and Kretsinger, R. H. (1994) Calcium-binding proteins 1: EF-hands. Protein 1, 343-517.
2. Ikura, M., and Ames, J. B. (2003) The role of calcium-binding proteins in the control of transcription: structure to function. Bioessays 24, 625-636.
3. Doanto, R., Haiech, J., Heizmann, C. W., and Gerke, V. (2000) in Calcium: The Molecular Basis of Calcium Action in Biology and Medicine, Kluwer Academic Publisher, Norwell, MA.
4. Carafoli, E. (2002) Calcium signaling: a tale for all seasons. Proc. Natl. Acad. Sci. U.S.A. 99, 1115-1122.
5. Thayer, S. A., Hirning, L. D., and Miller, R. J. (1988) The role of caffeine-sensitive calcium stores in the regulation of the intracellular free calcium concentration in rat sympathetic neurons in vitro. Mol. Pharmacol. 34, 664-673.
6. Trouslard, J., Marsh, S. J., and Brown, D. A. (1993) Calcium entry through nicotinic receptor channels and calcium channels in cultured rat superior cervical ganglion cells. J. Physiol. 468, 53-71.
7. Cheng, H., Lederer, W. J., and Cannell, M. B. (1993) Calcium sparks: elementary events underlying excitation-contraction coupling in heart muscle. Science 290, 740-744.
8. Toth, P. T., and Miller, R. J. (1995) Calcium and sodium currents evoked by action potential waveforms in rat sympathetic neurones. J. Physiol. 485, 43-57.
9. Rogers, M., and Dani, J. A. (1995) Comparison of quantitative calcium flux through NMDA, ATP, and ACh receptor channels. Biophys. J. 68, 501-506.
10. Berridge, M. J. (1995) Calcium signaling and cell proliferation. Bioessays 17, 491-500.
11. 2+-dependent block of CREB-CBP transcription by repressor DREAM. EMBO J. 21, 4583-4592.
12. 2+ binding and implications for kinase activation. Protein Sci. 6, 794-807.
13. 28k in cultured hippocampal neurons. Neuron 6, 41-51.
14. 2+ release in cardiac myocytes. Circ. Res. 91, 414-420.
15. Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution. Nature 405, 647-655.
16. Shapiro, L., Fannon, A. M., Kwong, P. D., Thompson, A., Lehmann, M. S., Legrand, J. F., Als-Nielsen, J., Colman, D. R., and Hendrickson, W. A. (1995) Structural basis of cell-cell adhesion by cadherins. Nature 374, 327-337.
17. Buxbaum, J. D., Choi, E. K., Luo, Y., Lilliehook, C., Crowley, A. C., Merriam, D. E., and Wasco, W. (1998) Calsenilin: a calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment. Nat. Med. 4, 1177-1181.
18. Dolmetsch, R. E., Pajvani, U., Fife, K., Spotts, J. M., and Greenberg, M. E. (2001) Signaling to the nucleus by an L-type calcium channel-calmodulin complex through the MAP kinase pathway. Science 294, 333-339.
19. Bruno, J., Horrocks, W. D., Jr., and Beckingham, K. (1996) Characterization of Eu(III) binding to a series of calmodulin binding site mutants using laser-induced Eu(III) luminescence spectroscopy. Biophys. Chem. 63, 1-16.
20. Sudnick, D. R., and Horrocks, W. D., Jr. (1979) Lanthanide ion probes of structure in biology. Environmentally sensitive fine structure in laser-induced terbium(III) luminescence. Biochim. Biophys. Acta 578, 135-144.
21. Lee, L., and Sykes, B. D. (1983) Use of lanthanide-induced nuclear magnetic resonance shifts for determination of protein structure in solution: EF calcium binding site of Carp Parvalbumin. Biochemistry 22, 4366-4373.
22. Geraldes, C. F. (1993) Lanthanide shift reagents. Methods Enzymol. 227, 43-78.
23. Bertini, I., Luchinat, C., and Rosato, A. (1996) The solution structure of paramagnetic metalloproteins. Prog. Biophys. Mol. Biol. 66, 43-80.
24. 1H NMR. Biochemistry 36, 11605-11618.
25. 9k. J. Biomol. NMR 21, 85-98.
26. Barbieri, R., Bertini, I., Cavallaro, G., Lee, Y. M., Luchinat, C., and Rosato, A. (2002) Paramagnetically induced residual dipolar couplings for solution structure determination of lanthanide-binding proteins. J. Am. Chem. Soc. 124, 5581-5587.
27. Geraldes, C. F. G. C., and Luchinat, C. (2003) Lanthanides as shift and relaxation agents in elucidating the structure of proteins and nucleic acids. Met. Ions Biol. Syst. 40, 513-588.
28. 3+ in a protozoan EF-hand calcium binding protein. Protein Sci. 12, 412-425.
29. Horrocks, W. D., Jr., and Tingey, J. M. (2003) Time-resolved europium(III) luminescence excitation spectroscopy: characterization of calcium-binding sites of calmodulin. Biochemistry 27, 413-419.
30. 15N relaxation using inverse detected two-dimensional NMR spectroscopy; the central helix is flexible. Biochemistry 31, 5269-5278.
31. Lee, L., and Sykes, B. D. (1981) Proton nuclear magnetic resonance determination of the sequential ytterbium replacement of calcium in carp parvalbumin. Biochemistry 20, 1156-1162.
32. 3+. FEBS Lett. 460, 519-526.
33. 2+ binding in calmodulin. Biochemistry 32, 7866-7871.
34. Studier, F. W., Rosenberg, A. H., Dunn, J. J., and Dubendorff, J. W. (1990) Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185, 60-89.
35. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) in Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory Press, New York.
36. Cai, M., Huang, Y., Sakaguchi, K., Clore, G. M., Gronenborn, A. M., and Craigie, R. (1998) An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli. J. Biomol. NMR 11, 97-102.
37. Gaberc-Porekar, V., and Menart, V. (2001) Perspectives of immobilized-metal affinity chromatography. J. Biochem. Biophys. Methods 49, 335-360.
38. Wang, C. L., Aquaron, R. R., Leavis, P. C., and Gergely, J. (1982) Metal-binding properties of calmodulin. Eur. J. Biochem. 124, 7-12.
39. Goddard, T. D., and Kneller, D. G. SPARKY 3, University of California, San Francisco. 2000. Computer Program.
40. Mulqueen, P., Tingey, J. M., and Horrocks, W. D., Jr. (1985) Characterization of lanthanide (III) ion binding to calmodulin using luminescence spectroscopy. Biochemistry 24, 6639-6645.
41. 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.
42. 2+ coordination. Biochemistry 37, 7617-7629.
43. Malmendal, A., Evenäs, J., Forsén, S., and Akke, M. (1999) Structural dynamics in the C-terminal domain of calmodulin at low calcium levels. J. Mol. Biol. 293, 883-899.
44. Allegrozzi, M., Bertini, I., Janik, M. B. L., Lee, Y.-M., Liu, G., and Luchinat, C. (2000) Lanthanide induced pseudocontact shifts for solution structure refinements of macromolecules in shells up to 40 A from the metal ion, J. Am. Chem. Soc. 122, 4154-4161.
45. Bertini, I., Luchinat, C., and Parigi, G. (2001) in Solution NMR of Paramagnetic Molecules, Elsevier, Amsterdam.
46. 15N spectra of larger proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin. Biochemistry 29, 4659-4667.
47. 2+ binding and conformational changes in a calmodulin domain. Biochemistry 37, 13744-13754.
48. Rawas, A., Moreton, K., Muirhead, H., and Williams, J. (1989) Preliminary crystallographic studies on duck ovotransferrin. J. Mol. Biol. 208, 213-214.
49. Evenäs, J., Forsén, S., Malmendal, A., and Akke, M. (1999) Backbone dynamics and energetics of a calmodulin domain mutant exchanging between closed and open conformations. J. Mol. Biol. 289, 603-617.
50. Atreya, H. S., Sahu, S. C., Bhattacharya, A., Chary, K. V. R., and Govil, G. (2001) NMR derived solution structure of an EF-hand calcium-binding protein from Entamoeba Histolytica. Biochemistry 40, 14392-14403.
51. VanScyoc, W. S., Sorensen, B. R., Rusinova, E., Laws, W. R., Ross, J. B., and Shea, M. A. (2002) Calcium binding to calmodulin mutants monitored by domain-specific intrinsic phenylalanine and tyrosine fluorescence. Biophys. J. 83, 2767-2780.
52. Wu, X., and Reid, B. R. (1997) Structure/calcium affinity relationships of site III of calmodulin: testing the acid pair hypothesis using calmodulin mutants. Biochemistry 36, 8649-8656.
53. 2+. Biochemistry 35, 5856-5869.
54. Wu, X., and Reid, R. E. (1997) Conservative D133E mutation of calmodulin site IV drastically alters calcium binding and phosphodiesterase regulation. Biochemistry 36, 3608-3616.
55. Bruno, J., Horrocks, W. D., Jr., and Zauhar, R. J. (1992) Europium(III) luminescence and tyrosine to terbium(III) energy-transfer studies of invertebrate (octopus) calmodulin. Biochemistry 31, 7016-7026.