Structure of the cytoplasmic domain of erythrocyte band 3 hereditary spherocytosis variant P327R: Band 3 Tuscaloosa

Biochemistry

Volumn 46, Issue 36, 2007, Pages 10248-10257

  Zhou, Zheng ^a   DeSensi, Susan C ^b   Stein, Richard A ^a   Brandon, Suzanne ^a   Song, Likai ^c   Cobb, Charles E ^a   Hustedt, Eric J ^a   Beth, Albert H ^a  

^a VANDERBILT UNIVERSITY   (United States)

^b VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c FLORIDA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; CELL MEMBRANES; DIMERS; DISEASES; DISSOCIATION; MUTAGENESIS; PARAMAGNETIC RESONANCE;

BINDING SURFACES; DOUBLE ELECTRON-ELECTRON RESONANCE (DEER); ERYTHROCYTES; POINT MUTATION; PROTEIN STRUCTURE;

BLOOD;

ERYTHROCYTE BAND 3 PROTEIN; MEMBRANE PROTEIN; ARGININE; BAND 3 PROTEIN TUSCALOOSA; DRUG DERIVATIVE; EDDA; EDETIC ACID; MUTANT PROTEIN; PROLINE; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; CYTOPLASM; DIMERIZATION; ELECTRON SPIN RESONANCE; ERYTHROCYTE MEMBRANE; HEMOLYTIC ANEMIA; HUMAN; MISSENSE MUTATION; POINT MUTATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; SPECTROSCOPY; SPHEROCYTOSIS; SPIN LABELING; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HEREDITARY SPHEROCYTOSIS; METABOLISM; MUTATION; NORMAL DISTRIBUTION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

ANION EXCHANGE PROTEIN 1, ERYTHROCYTE; ARGININE; CYTOPLASM; DIMERIZATION; EDETIC ACID; ELECTRON SPIN RESONANCE SPECTROSCOPY; HUMANS; MODELS, MOLECULAR; MUTANT PROTEINS; MUTATION; NORMAL DISTRIBUTION; PROLINE; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SPECTRUM ANALYSIS; SPHEROCYTOSIS, HEREDITARY; SPIN LABELS;

EID: 35148883146     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700948p     Document Type: Article

References (55)

1. Skalak, R., and Branemark, P. I. (1969) Deformation of red blood cells in capillaries, Science 164, 717-719.
2. Tanner, M. J. (2002) Band 3 anion exchanger and its involvement in erythrocyte and kidney disorders, Curr. Opin. Hematol. 9, 133-139.
3. Tse, W. T., Lecomte, M. C., Costa, F. F., Garbarz, M., Feo, C., Boivin, P., Dhermy, D., and Forget, B. G. (1990) Point mutation in the β-spectrin gene associated with α I/74 hereditary elliptocytosis. Implications for the mechanism of spectrin dimer self-association, J. Clin. Invest. 86, 909-916.
4. Feo, C. J., Fischer, S., Piau, J. P., Grange, M. J., and Tchernia, G. (1980) First instance of the absence of an erythrocyte membrane protein (band 4(1)) in a case of familial elliptocytic anemia, Nouv. Rev. Fr. Hematol. 22, 315-325.
5. Tchernia, G., Mohandas, N., and Shohet, S. B. (1981) Deficiency of skeletal membrane protein band 4.1 in homozygous hereditary elliptocytosis. Implications for erythrocyte membrane stability, J. Clin. Invest. 68, 454-460.
6. Conboy, J., Mohandas, N., Tchernia, G., and Kan, Y. W. (1986) Molecular basis of hereditary elliptocytosis due to protein 4.1 deficiency, N. Engl. J. Med. 315, 680-685.
7. Gallagher, P. G., and Ferriera, J. D. (1997) Molecular basis of erythrocyte membrane disorders, Curr. Opin. Hematol. 4, 128-135.
8. Delaunay, J. (2002) Molecular basis of red cell membrane disorders, Acta Haematol. 108, 210-218.
9. Bennett, V., and Baines, A. J. (2001) Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues, Physiol. Rev. 81, 1353-1392.
10. Birkenmeier, C. S., and Barker, J. E. (2004) Hereditary haemolytic anaemias: unexpected sequelae of mutations in the genes for erythroid membrane skeletal proteins, J. Pathol. 204, 450-459.
11. Tanner, M. J. (1997) The structure and function of band 3 (AE1): recent developments (review), Mol. Membr. Biol. 14, 155-165.
12. Fairbanks, G., Steck, T. L., and Wallach, D. F. (1971) Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane, Biochemistry 10, 2606-2617.
13. Steck, T. L., Ramos, B., and Strapazon, E. (1976) Proteolytic dissection of band 3, the predominant transmembrane polypeptide of the human erythrocyte membrane, Biochemistry 15, 1153-1161.
14. Tanner, M. J., Martin, P. G., and High, S. (1988) The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequence, Biochem. J. 256, 703-712.
15. Lux, S. E., John, K. M., Kopito, R. R., and Lodish, H. F. (1989) Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1), Proc. Natl. Acad. Sci. U.S.A. 86, 9089-9093.
16. Lepke, S., and Passow, H. (1976) Effects of incorporated trypsin on anion exchange and membrane proteins in human red blood cell ghosts, Biochim. Biophys. Acta 455, 353-370.
17. Grinstein, S., Ship, S., and Rothstein, A. (1978) Anion transport in relation to proteolytic dissection of band 3 protein, Biochim. Biophys. Acta 507, 294-304.
18. Low, P. S. (1986) Structure and function of the cytoplasmic domain of band 3: center of erythrocyte membrane-peripheral protein interactions, Biochim. Biophys. Acta 864, 145-167.
19. Bennett, V., and Stenbuck, P. J. (1980) Association between ankyrin and the cytoplasmic domain of band 3 isolated from the human erythrocyte membrane, J. Biol. Chem. 255, 6424-6432.
20. Rybicki, A. C., Schwartz, R. S., Hustedt, E. J., and Cobb, C. E. (1996) Increased rotational mobility and extractability of band 3 from protein 4.2-deficient erythrocyte membranes: evidence of a role for protein 4.2 in strengthening the band 3-cytoskeleton linkage, Blood 88, 2745-2753.
21. Pasternack, G. R., Anderson, R. A., Leto, T. L., and Marchesi, V. T. (1985) Interactions between protein 4.1 and band 3. An alternative binding site for an element of the membrane skeleton, J. Biol. Chem. 260, 3676-3683.
22. Low, P. S., Willardson, B. M., Mohandas, N., Rossi, M., and Shohet, S. (1991) Contribution of the band 3-ankyrin interaction to erythrocyte membrane mechanical stability, Blood 77, 1581-1586.
23. Peters, L. L., Shivdasani, R. A., Liu, S. C., Hanspal, M., John, K. M., Gonzalez, J. M., Brugnara, C., Gwynn, B., Mohandas, N., Alper, S. L., Orkin, S. H., and Lux, S. E. (1996) Anion exchanger 1 (band 3) is required to prevent erythrocyte membrane surface loss but not to form the membrane skeleton, Cell 86, 917-927.
24. Southgate, C. D., Chishti, A. H., Mitchell, B., Yi, S. J., and Palek, J. (1996) Targeted disruption of the murine erythroid band 3 gene results in spherocytosis and severe haemolytic anaemia despite a normal membrane skeleton, Nat. Genet. 14, 227-230.
25. Moriyama, R., Ideguchi, H., Lombardo, C. R., Van Dort, H. M., and Low, P. S. (1992) Structural and functional characterization of band 3 from Southeast Asian ovalocytes, J. Biol. Chem. 267, 25792-25797.
26. Schofield, A. E., Tanner, M. J., Pinder, J. C., Clough, B., Bayley, P. M., Nash, G. B., Dluzewski, A. R., Reardon, D. M., Cox, T. M., and Wilson, R. J. (1992) Basis of unique red cell membrane properties in hereditary ovalocytosis, J. Mol. Biol. 223, 949-958.
27. Gallagher, P. G., and Forget, B. G. (1997) Hematologically important mutations: band 3 and protein 4.2 variants in hereditary spherocytosis, Blood Cells Mol. Dis. 23, 417-421.
28. Jarolim, P., Palek, J., Rubin, H. L., Prchal, J. T., Korsgren, C., and Cohen, C. M. (1992) Band 3 Tuscaloosa: Pro327-Arg327 substitution in the cytoplasmic domain of erythrocyte band 3 protein associated with spherocytic hemolytic anemia and partial deficiency of protein 4.2, Blood 80, 523-529.
29. Zhang, D., Kiyatkin, A., Bolin, J. T., and Low, P. S. (2000) Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3, Blood 96, 2925-2933.
30. Zhou, Z., DeSensi, S. C., Stein, R. A., Brandon, S., Dixit, M., McArdle, E. J., Warren, E. M., Kroh, H. K., Song, L., Cobb, C. E., Hustedt, E. J., and Beth, A. H. (2005) Solution structure of the cytoplasmic domain of erythrocyte membrane band 3 determined by site-directed spin labeling, Biochemistry 44, 15115-15128.
31. Low, P. S., Zhang, D., and Bolin, J. T. (2001) Localization of mutations leading to altered cell shape and anion transport in the crystal structure of the cytoplasmic domain of band 3, Blood Cells Mol. Dis. 27, 81-84.
32. Zhou, Z., Desensi, S., Brandon, S., Dixit, N., Cobb, C. E., Hustedt, E. J., and Beth, A. H. (2005) Solution structure of cdb3 from site directed spin labeling studies and double electron-electron resonance, Biophys. J. 88, 265a (abstract).
33. Bustos, S. P., and Reithmeier, R. A. (2005) Molecular characterization of hereditary spherocytosis mutants in the cytosolic domain of the erythrocyte Cl-/HCO3-anion exchanger, Biophys. J. 88, 224a (abstract).
34. Bustos, S. P., and Reithmeier, R. A. (2006) Structure and stability of hereditary spherocytosis mutants of the cytosolic domain of the erythrocyte anion exchanger 1 protein, Biochemistry 45, 1026-1034.
35. Studier, F. W. (2005) Protein production by auto-induction in high-density shaking cultures, Protein Expr. Purif. 41, 207-234.
36. Altenbach, C., Froncisz, W., Hemker, R., McHaourab, H., and Hubbell, W. L. (2005) Accessibility of nitroxide side chains: absolute Heisenberg exchange rates from power saturation EPR, Biophys. J. 89, 2103-2112.
37. Subczynski, W. K., and Hyde, J. S. (1981) The diffusion-concentration product of oxygen in lipid bilayers using the spin-label T1 method, Biochim. Biophys. Acta 643, 283-291.
38. Altenbach, C., Flitsch, S. L., Khorana, H. G., and Hubbell, W. L. (1989) Structural studies on transmembrane proteins. 2. Spin labeling of bacteriorhodopsin mutants at unique cysteines, Biochemistry 28, 7806-7812.
39. Pannier, M., Veit, S., Godt, A., Jeschke, G., and Spiess, H. W. (2000) Dead-time free measurement of dipole-dipole interactions between electron spins, J. Magn. Reson. 142, 331-340.
40. Jeschke, G. (2002) Determination of the nanostructure of polymer materials by electron paramagnetic resonance spectroscopy, Macromol. Rapid Commun. 23, 227-246.
41. Jeschke, G. (2002) Distance measurements in the nanometer range by pulse EPR, ChemPhysChem 3, 927-932.
42. Jeschke, G., Koch, A., Jonas, U., and Godt, A. (2002) Direct conversion of EPR dipolar time evolution data to distance distributions, J. Magn. Reson. 155, 72-82.
43. McHaourab, H. S., Lietzow, M. A., Hideg, K., and Hubbell, W. L. (1996) Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics, Biochemistry 35, 7692-7704.
44. Columbus, L., and Hubbell, W. L. (2002) A new spin on protein dynamics, Trends Biochem. Sci. 27, 288-295.
45. Feix, J. B., and Klug, C. S. (1998) Site-directed spin labeling of membrane proteins and membrane interactions, Biological Magnetic Resonance, pp 251-281, Plenum Press, New York.
46. Hubbell, W. L., Cafiso, D. S., and Altenbach, C. (2000) Identifying conformational changes with site-directed spin labeling, Nat. Struct. Biol. 7, 735-739.
47. Richardson, J. S. (1981) The anatomy and taxonomy of protein structure, Adv. Protein Chem. 34, 167-339.
48. Aurora, R., and Rose, G. D. (1998) Helix capping, Protein Sci. 7, 21-38.
49. Gellman, S. H. (1998) Minimal model systems for β sheet secondary structure in proteins, Curr. Opin. Chem. Biol. 2, 717-725.
50. Crespo, M. D., Platt, G. W., Bofill, R., and Searle, M. S. (2004) Context-dependent effects of proline residues on the stability and folding pathway of ubiquitin, Eur. J. Biochem. 271, 4474-4484.
51. Hustedt, E. J., Stein, R. A., Sethaphong, L., Brandon, S., Zhou, Z., and Desensi, S. C. (2006) Dipolar coupling between nitroxide spin labels: the development and application of a tether-in-a-cone model, Biophys. J. 90, 340-356.
52. Rabenstein, M. D., and Shin, Y. K. (1995) Determination of the distance between two spin labels attached to a macromolecule, Proc. Natl. Acad. Sci. U.S.A. 92, 8239-8243.
53. Pyka, J., Ilnicki, J., Altenbach, C., Hubbell, W. L., and Froncisz, W. (2005) Accessibility and dynamics of nitroxide side chains in T4 lysozyme measured by saturation recovery EPR, Biophys. J. 89, 2059-2068.
54. Korsgren, C., and Cohen, C. M. (1988) Associations of human erythrocyte band 4.2. Binding to ankyrin and to the cytoplasmic domain of band 3, J. Biol. Chem. 263, 10212-10218.
55. Langen, R., Oh, K. J., Cascio, D., and Hubbell, W. L. (2000) Crystal structures of spin labeled T4 lysozyme mutants: implications for the interpretation of EPR spectra in terms of structure, Biochemistry 39, 8396-8405.