Membrane-inserted conformation of transmembrane domain 4 of divalent-metal transporter

Biochemical Journal

Volumn 372, Issue 3, 2003, Pages 757-766

  Li, Hongyan ^a   Li, Fei ^b   Sun, Hongzhe ^b   Qian, Zhong Ming ^a  

^a HONG KONG POLYTECHNIC UNIVERSITY   (Hong Kong)

^b UNIVERSITY OF HONG KONG   (Hong Kong)

Author keywords

Circular dichroism (CD); Detergent; Divalent metal transporter 1 (DMT1); NMR; Phospholipid vesicles; Secondary structure

Indexed keywords

HYDROPHOBICITY; MICELLES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH EFFECTS; PHOSPHOLIPIDS; PROTEINS;

TRANSMEMBRANES;

BIOLOGICAL MEMBRANES;

1,2 DIMYRISTOYLGLYCERO 3 [PHOSPHORAC (1 GLYCEROL)]; ANION; DIMYRISTOYLPHOSPHATIDYLCHOLINE; DIMYRISTOYLPHOSPHATIDYLGLYCEROL; DODECYL SULFATE SODIUM; DODECYLPHOSPHORYLCHOLINE; LYSINE; MEMBRANE PROTEIN; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 2; PHOSPHOLIPID; PROTON; STEARIC ACID DERIVATIVE; TRIFLUOROETHANOL; UNCLASSIFIED DRUG; VALINE;

ACIDITY; ALPHA HELIX; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; ELECTRICITY; HYDROPHOBICITY; LAMELLAR BODY; MEMBRANE BINDING; MICELLE; MOLECULAR MIMICRY; MOLECULAR PROBE; MOLECULAR STABILITY; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; NUCLEOTIDE SEQUENCE; PHOSPHOLIPID VESICLE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; SIMULATION; SURFACE PROPERTY; TEMPERATURE DEPENDENCE;

AMINO ACID SEQUENCE; ANIMALS; CATION TRANSPORT PROTEINS; CIRCULAR DICHROISM; DETERGENTS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HUMANS; HYDROGEN-ION CONCENTRATION; IRON-BINDING PROTEINS; MEMBRANES, ARTIFICIAL; MICELLES; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; SODIUM DODECYL SULFATE; TRIFLUOROETHANOL;

EID: 0038266898     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20030075     Document Type: Article

References (64)

1. Richardson, D. R. and Ponka, P. (1997) The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells. Biochim. Biophys. Acta 1331, 1-40
2. Qian, Z. M., Wang, Q. and Tang, P. L. (1997) Iron crossed the endosomal membrane by a carrier-mediated process. Prog. Biophys. Mol. Biol. 87, 1-15
3. Sun, H. Z., Li, H. Y. and Sadler, P. J. (1999) Transferrin as a metal ion mediator. Chem. Rev. 99, 2817-2842
4. Li, H. Y., Sun, H. Z. and Qian, Z. M. (2002) The role of the transferrin-transferrin-receptor system in drug delivery and targeting. Trends Pharmacol. Sci. 23, 206-209
5. Andrews, N. C. (1999) Disorders of iron metabolism. New Engl. J. Med. 341, 1986-1995
6. Smith, M. A., Harris, P. L. R., Sayre, L. M. and Perry, G. (1997) Iron accumulation in Alzheimer disease is a source of redox-generated free radicals. Proc. Natl. Acad. Sci. U.S.A. 94, 9866-9868
7. Gunshin, H., Mackenzie, B., Berger, U. V., Gunshin, Y., Romero, M. F., Boron, W. F., Nussberger, S., Gollan, J. L. and Hediger, M. A. (1997) Cloning and characterization of a mammalian proton-coupled metal-ion transporter. Nature (London) 388, 482-488
8. Fleming, M. D., Trenor, C. C., Su, M. A., Foernzler, D., Beier, D. R., Dietrich, W. F. and Andrews, N. C. (1997) Microcytic anemia mice have a mutation in Nramp2, a candidate iron transporter gene. Nat. Genet. 18, 383-386
9. Feder, J. N., Gnirke, A., Thomas, W., Tsuchihashi, Z., Ruddy, D. A., Basava, A., Dormishian, F., Domingo, Jr, R., Ellis, M. C., Fullan, A. et al (1996) A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis. Nat. Genet. 13, 399-408
10. Donovan, A., Brownlie, A., Zhou, Y., Shepard, J., Pratt, S. J., Moynihan, J., Paw, B. H., Drejer, A., Barut, B., Zapata, A. et al. (2000) Positional cloning of zebrafish ferroportin 1 identifies a conserved vertebrate iron exporter Nature (London) 483, 776-781
11. Fleming, M. D., Romano, M. A., Su, M. A., Garrick, L. M., Garrick, M. D. and Andrews, N. C. (1998) Nramp2 is mutated in the anemia Belgrade (b) rat: evidence of a role for Nramp2 in endosomal iron transport. Proc. Natl. Acad. Sci. U.S.A. 95 1148-1153
12. Su, M. A., Trenor, C. C., Fleming, J. C., Fleming, M. D. and Andrews, N. C. (1998) The G185R mutation disrupts function of the iron transporter Nramp2. Blood 92, 2157-2163
13. Xie, H., Ding, F. X., Schreiber, D., Eng, G., Liu, S. F., Arshava, B., Arevalo, E., Becket, J. M. and Naider, F. (2000) Synthesis and biophysical analysis of transmembrane domains of a Saccharomyces cerevisiae G protein-coupled receptor. Biochemistry 39, 15462-15474
14. Ding, F. X., Xie, H., Arshava, B., Becker, J. F. and Naider, F. (2001) ATR-FTIR study of the structure and orientation of transmembrane domains of the Saccharomyces cerevisiae α-mating factor receptor in phospholipids. Biochemistry 40, 8945-8954
15. Sorgen, P. L., Hu, Y., Guan, L., Kaback, H. R. and Girvin, M. E. (2002) An approach to membrane protein structure without crystals. Proc. Natl. Acad. Sci. U.S.A. 99, 14037-14040
16. Opella, S. J., Marassi, F. M., Gesell, J. J., Valente, A. P., Kim, Y., Oblatt-Montal, M. and Montal, M. (1999) Structures of the M2 channel-lining segments from nicotinic acetycholine and NMDA receptors by NMR spectroscopy. Nat. Struct. Biol. 6, 374-379
17. MacKenzie, K. R., Prestegard, J. H. and Engelman, D. M. (1997) A transmembrane helix dimer: structure and implications. Science 276, 131-133
18. Schulz, A., Bruns, K., Henklein, P., Krause, G., Schubert, M., Gudermann, T., Wray, V., Schultz, G. and Schöneberg, T. (2000) Requirement of specific intrahelical interactions for stabilizing the inactive conformation of glycoprotein hormone receptor. J. Biol. Chem. 275, 37860-37869
19. Rozek, A., Friedrich, C. L. and Hancock, R. E. W. (2000) Structure of the bovine anti-microbial peptide indolicdin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles. Biochemistry 39, 15765-15774
20. Hunt, J. F., Earnest, T. N., Bousche, O., Kalghatgi, K., Reilly, K., Horvath, C., Rothschild, K. J. and Engelman, D. M. (1997) A biophysical study of integral membrane protein folding. Biochemistry 38, 15156-15176
21. Wigley, W. C., Vijayakumar, S., Jones, J. D., Slaughter, C. and Thomas, P. J. (1998) Transmembrane domain of cystic fibrosis transmembrane conductance regulator: design, characterization, and secondary structure of synthetic peptides m1-m6. Biochemistry 37, 844-853
22. Oblatt-Montal, M., Reddy, G. L., Iwamoto, T., Tomich, J. M. and Montal, M. (1994) Identification of anion channel-forming motif in the primary structure of CFTR, the cystic-fibrosis chloride channel. Proc. Natl. Acad. Sci. U.S.A. 91, 1495-1499
23. Killian, J. A., Trouard, T. P., Greathouse, D. V., Chupin, V. and Lindblom, G. (1994) A general method for the preparation of mixed micelles of hydrophobic peptides and sodium dodecyl sulphate. FEBS Lett. 348, 161-165
24. MacDonald, R. I. and MacDonald, R. C. (1975) Assembly of phospholipid vesicles bearing sialoglycoprotein from erythrocyte membrane. J. Biol. Chem. 250, 9206-9214
25. Liu, L. P., Li, S. C., Goto, N. K. and Deber, C. M. (1996) Threshold hydrophobicity dictates helical conformations of peptides in membrane environments. Biopolymer 39, 465-470
26. Bax, A. and Davis, D. G. (1985) MLEV-17-based two-dimensional homo-nuclear magnetization transfer spectroscopy. J. Magn. Reson. 65, 355-360
27. Jeener, J., Meier, B. H., Bachmann, P. and Ernst, R. R. (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71, 4546-4553
28. Piotto, M., Saudek, V. and Sklenar, V. (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of a aqueous solutions. J. Biol. NMR 2, 661-665
29. Sreerama, N. and Woody, R. W. (2000) Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287, 252-260
30. Provencher, S. W. and Glockner, J. (1981) Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20, 33-37
31. Wu, C. S. C., Ikeda, K. and Yang, J. T. (1981) Ordered conformation of polypeptides and proteins in acidic dodecyl sulfate solution. Biochemistry 20, 566-570
32. Chen, Y. H., Yang, J. T. and Chau, K. H. (1974) Determination of the helix and β form of proteins in aqueous solution by circular dichroism. Biochemistry 13, 3350-3359
33. Schägger, H. and von Jagow, G. (1987) Tricine sodium dodecyl sulfate polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 kDa to 100 kDa. Anal. Biochem. 186, 368-379
34. Zhong, L. X. and Johnson, Jr, W. C. (1992) Environment effects amino acid preference for secondary structure. Proc. Natl. Acad. Sci. U.S.A. 89, 4462-4465
35. Watson, R. M., Woody, R. W., Lewis, R. V., Bohle, D. S., Andreotti, A. H., Ray, B. and Miller, K. W. (2001) Conformational changes in pediocin AcH upon vesicle binding and approximation of the membrane-bound structure in detergent micelles. Biochemistry 40, 14037-14046
36. Lauterwein, J., Bosch, C., Brown, L. R. and Wüthrich, K. (1979) Physicochemical studies of the protein-lipid interactions in melittin-containing micelles. Biochim. Biophys. Acta 558, 244-246
37. Wallace, B. A. and Mao, D. (1984) Circular dichroism analyses of membrane proteins - an estimation of differential light scattering and absorption flattening effects in large membrane vesicles and membrane sheets. Anal. Biochem. 142, 317-328
38. Wüthrich, K. (1986) NMR of Protons and Nucleic Acids, Wiley, New York
39. Wishart, D. S., Sykes, B. D. and Richards, F. M. (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31, 1647-1651
40. Wüthrich, K., Billeter, M. and Braun, W. (1984) Poly-peptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distance. J. Mol. Biol. 180, 715-740
41. 1H nuclear magnetic resonance spectra. Computation of sterically allowed proton-proton distance and statistical analysis of proton-proton distance in single crystal protein comformations. J. Mol. Biol. 155, 321-346
42. Papavoine, C. H. M., Konings, R. N. H., Hilbers, C. W. and van de Ven, F. J. M. (1994) Location of M13 coated protein in sodium dodecyl sulfate micelles as determined by NMR. Biochemistry 33, 12990-12997.
43. 1H NMR study. Biochemistry 34, 11617-11624
44. 1H NMR. Biochemistry 36, 8153-8163
45. Lindberg, M., Jarvet, J., Langel, Ü. and Gräslund, A. (2001) Secondary structure and position of the cell-penetrating peptide transportan in SDS micelles as determined by NMR. Biochemistry 40, 3141-3149
46. Avrahami, D., Oren, Z. and Shai, Y. (2001) Effect of multiple aliphatic amino acids substitutions on the structure, function, and mode of action of diastereomeric membrane active peptides. Biochemistry 40, 12591-12603
47. Melnyk, R. A., Partridge, A. W. and Deber, C. M. (2001) Retention of native-like oligomerization states in transmembrane segment peptides: application to the Escherichia coli aspartate receptor. Biochemistry 40, 11106-11113
48. Albert, A. D. and Yeagle, P. L. (2000) Domain approach to three dimensional structure of rhodopsin using high resolution nuclear magnetic resonance. Methods Enzymol. 315, 107-115
49. Aggeli, A., Bannister, M. L., Bell, M., Boden, N., Findlay, J. B. C., Hunter, M., Knowles, P. F. and Yang, J. C. (1998) Conformational and ion-channeling activity of a 27-residue peptide modeled on the single-transmembrane segment of the IsK (minK) protein. Biochemistry 37, 8121-8131
50. Martin, N. P., Leavitt, L. M. Sommers, C. M. and Dumont, M. E. (1999) Assembly of G protein-coupled receptor from fragments: Identification of functional receptors with discontinuities in each of the loops connecting transmembrane segments. Biochemistry 38, 682-695
51. Ridge, K. D., Lee, S. S. and Yao, L. L. (1995) In vivo assembly of rhodopsin from expressed polypeptide fragments. Proc. Natl. Aacd. Sci. U.S.A. 92, 3204-3208
52. Engelman, D. M., Steitz, T. A. and Goldman, A. (1986) Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins. Annu. Rev. Biophys. Biophys. Chem. 15, 321-353
53. Adair, B. D. and Engelman, D. M. (1994) Glycophorin A helical transmembrane domains dimerize in phospholipid bilayers - a resonance energy transfer study. Biochemistry 33, 5539-5544
54. Ladokhin, A. S., Selsted, M. E. and White, S. H. (1999) CD spectra of indolicidin antimicrobial peptides suggest turns, not polyproline helix. Biochemistry 38, 12313-12319
55. Aivazian, D. and Stern, L. J. (2000) Phosphorylation of T cell receptor is ζ regulated by a lipid dependent folding transition. Nat. Struct. Biol. 7, 1023-1026
56. Garavito, R. M. and Ferguson-Miller, S. (2001) Detergents as tools in membrane biochemistry. J. Biol. Chem. 276, 32403-32406
57. Liu, L. P. and Deber, C. M. (1997) Anionic phospholipids modulate peptide insertion into membranes. Biochemistry 36, 5476-5482
58. Kim, J. Y., Blackshear, P. J., Johnson, J. D. and Mclaughlin, S. (1994) Phosphorylation reverses the membrane association of peptides that correspond to the basic domains of MARCKS and neuromodulin. Biophys. J. 67, 227-237
59. Breukink, E., Demel, R. A., de Korte-Kool, G. and de Kruijff, B. (1992) SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP - a monolayer study. Biochemistry 31, 1119-1124
60. Han, X., Bushweller, J. H., Cafiso, D. S. and Tamm, L. K. (2001) Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin. Nat. Struct. Biol. 8, 715-720
61. Han, X. and Tamm, L. K. (2000) A host-guest system to study structure-function relationships of membrane fusion peptides. Proc. Natl. Acad. Sci. U.S.A. 97, 13097-13102
62. Han, X. and Tamm, L. K. (2000) pH-dependent self-association of influenza hemagglutinin fusion peptides in lipids bilayers. J. Mol. Biol. 304, 953-965
63. Bader, R., Bettio, A., Beck-Sickinger, A. G. and Zerbe, O. (2001) Structure and dynamics of micelle-bound neuropeptide Y: comparison with unligated NPY and implications for receptor selection. J. Mol. Biol. 305, 307-329
64. Öhman, A., Lycksell, P., Juréus, A., Langel, Ö., Bartfai, T. and Gräslund, A. (1998) NMR study of the conformation and localization of porcine galanin in SDS micelles. Comparison with an inactive analog and a galanine receptor antagonist. Biochemistry 37, 9169-9178