Initiation and propagation of spectrin heterodimer assembly involves distinct energetic processes

Biochemistry

Volumn 46, Issue 37, 2007, Pages 10585-10594

  Li, Donghai ^a   Harper, Sandra ^a   Speicher, David W ^a  

^a WISTAR INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING DOMAIN; HOMODIMERS; ISOTHERMAL TITRATION CALORIMETRY; SPECTRIN HETERODIMER ASSEMBLY;

CALORIMETRY; CYTOLOGY; DIMERIZATION; HYDROGEN BONDS; MOLECULAR STRUCTURE; TITRATION;

DIMERS;

ACTIN BINDING PROTEIN; DIMER; FODRIN; HETERODIMER; HISTIDINE; SPECTRIN; SPECTRIN BETA SUBUNIT; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; DIMERIZATION; ELECTRICITY; ENERGY TRANSFER; ENTHALPY; ENTROPY; HYDROGEN BOND; HYDROPHILICITY; HYDROPHOBICITY; ISOTHERMAL TITRATION CALORIMETRY; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; STOICHIOMETRY; THERMODYNAMICS;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BUFFERS; CALORIMETRY; CHICKENS; DIMERIZATION; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN BINDING; PROTEIN FOLDING; PROTONS; RECOMBINANT PROTEINS; SPECTRIN; TEMPERATURE; THERMODYNAMICS;

EID: 34548767082     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7007905     Document Type: Article

References (37)

1. Marchesi, V. T., and Steers, E. (1968) Selective solubilization of a protein component of the red cell membrane, Science 159, 203-204.
2. Clarke, M. (1971) Isolation and characterization of a water-soluble protein from bovine erythrocyte membranes, Biochem. Biophys. Res. Commun. 45, 1063-1070.
3. Fairbanks, G., Steck, T. L., and Wallach, D. F. H. (1971) Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane, Biochemistry 10, 2606-2617.
4. Shotton, D. M., Burke, B. E., and Branton, D. (1979) The molecular structure of human erythrocyte spectrin - Biophysical and electron microscopic studies, J. Mol. Biol. 131, 303-329.
5. Speicher, D. W., and Marchesi, V. T. (1984) Erythrocyte spectrin is comprised of many homologous triple helical segments, Nature 311, 177-180.
6. Yan, Y., Winograd, E., Viel, A., Cronin, T., Harrison, S. C., and Branton, D. (1993) Crystal structure of the repetitive segments of spectrin, Science 262, 2027-2030.
7. Tang, H.-Y., and Speicher, D. W. (2004) In vivo phosphorylation of human erythrocyte spectrin occurs in a sequential manner, Biochemistry 43, 4251-4262.
8. Speicher, D. W., Weglarz, L., and Desilva, T. M. (1992) Properties of human red-cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site, J. Biol. Chem. 267, 14775-14782.
9. V/41 polymorphism) and intron 45 and with partial skipping of exon 46, J. Clin. Invest. 91, 2091-2096.
10. Wilmotte, R., Harper, S. L., Ursitti, J. A., Marechal, J., Delaunay, J., and Speicher, D. W. (1997) Exon 46-encoded sequence is essential for stability of human erythroid alpha-spectrin and heterodimer formation, Blood 90, 4188-4196.
11. Ursitti, J. A., Kotula, L., DeSilva, T. M., Curtis, P. J., and Speicher, D. W. (1996) Mapping the human erythrocyte β-Spectrin dimer initiation site using recombinant peptides and correlation of its phasing with the α-actinin dimer site, J. Biol. Chem. 271, 6636-6644.
12. Harper, S. L., Begg, G. E., and Speicher, D. W. (2001) Role of terminal nonhomologous domains in initiation of human red cell spectrin dimerization, Biochemistry 40, 9935-9943.
13. Viel, A., and Branton, D. (1994) Interchain binding at the tail end of the Drosophila spectrin molecule, Proc. Natl. Acad. Sci. U.S.A. 91, 10839-10843.
14. Viel, A., Gee, M. S., Tomooka, L., and Branton, D. (1998) Motifs involved in interchain binding at the tail-end of spectrin, Biochim. Biophys. Acta 1384, 396-404.
15. Begg, G. E., Harper, S. L., Morris, M. B., and Speicher, D. W. (2000) Initiation of spectrin dimerization involves complementary electrostatic interactions between paired triple-helical bundles, J. Biol. Chem. 275, 3279-3287.
16. Law, R., Harper, S. L., Speicher, D. W., and Discher, D. E. (2004) Influence of lateral association on forced unfolding of antiparallel spectrin heterodimers, J. Biol. Chem. 279, 16410-16416.
17. Riahi, M. H., Kakhniashvili, D. G., and Goodman, S. R. (2005) Ubiquitination of red blood cell α-spectrin does not affect heterodimer formation, Am. J. Hematol. 78, 281-287.
18. Goodman, S. R., Pace, B. S., and Shartava, A. (1999) New therapeutic approaches to sickle cell disease: Targeting RBC membrane oxidative damage, Cell. Mol. Biol. Lett. 3, 403-411.
19. Monterio, C. A., Gibson, X. A., Shartava, A., and Goodman, S. R. (1998) Preliminary characterization of a structural defect in homozygous sickle cell a-spectrin demonstrated by a rabbit autoantibody, Am. J. Hematol. 58, 200-205.
20. Sangerman, J., Kakhniashvili, D., Brown, A., Shartava, A., and Goodman, S. R. (2001) Spectrin ubiquitination and oxidative stress: potential roles in blood and neurological disorders, Cell. Mol. Biol. Lett. 6, 607-636.
21. Grum, V. L., Li, D. N., MacDonald, R. I., and Mondragon, A. (1999) Structures of two repeats of spectrin suggest models of flexibility, Cell 98, 523-535.
22. Kusunoki, H., Minasov, G., MacDonald, R. I., and Mondragon, A. (2004) Independent movement, dimerization and stability of tandem repeats of chicken brain α-spectrin, J. Mol. Biol. 344, 495-511.
23. Kusunoki, H., MacDonald, R. I., and Mondragon, A. (2004) Structural insights into the stability and flexibility of unusual erythroid spectrin repeats, Structure 12, 645-656.
24. Djinovic-Carugo, K., Young, P., Gautel, M., and Saraste, M. (1999) Structure of the α-actinin rod: Molecular basis for cross-linking of actin filaments, Cell 98, 537-546.
25. Ylanne, J., Scheffzek, K., Young, P., and Saraste, M. (2001) Crystal structure of the α-actinin rod reveals an extensive torsional twist, Structure 9, 597-604.
26. Wiseman, T., Williston, S., Brandts, J. F., and Lin, L. N. (1989) Rapid measurement of binding constants and heats of binding using a new titration calorimeter, Anal. Biochem. 179, 131-137.
27. Arnold, K., Bordoli, L., Kopp, J., and Schwede, T. (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modeling, Bioinformatics 22, 195-201.
28. Sali, A., and Blundell, T. L. (1993) Comparative protein modeling by satisfaction of spatial restraints, J. Mol. Biol. 234, 779-815.
29. Chenna, R., Sugawara, H., Koike, T., Lopez, R., Gibson, T. J., Higgins, D. G., and Thompson, J. D. (2003) Multiple sequence alignment with the Clustal series of programs, Nucleic Acids Res. 31, 3497-3500.
30. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
31. DeLano, W. L. (2004) The PyMOL molecular graphics system user's manual, DeLano Scientific, San Carlos, CA.
32. Bates, R. G., and Hetzer, H. B. (1961) Dissociation constant of protonated acid form of 2-amino-2-(hydroxymethyl)-1,3-propanediol [tris-hydroxymethyl)-aminomethane] and related thermodynamic quantities from 0 to 50°, J. Phys. Chem. 65, 667-671.
33. Baker, B. M., and Murphy, K. P. (1996) Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry, Biophys. J. 71, 2049-2055.
34. Murphy, K. P., Xie, D., Thompson, K. S., Amzel, L. M., and Freire, E. (1994) Entropy in biological binding processes - estimation of translational entropy loss, Proteins 18, 63-67.
35. Winzor, D. J., and Sawyer, W. H. (1995) Quantitative characterization of ligand binding, pp 1-2, John Wiley and Sons, Inc., New York.
36. Jacobson, T., Williamson, J., Wasilewski, A., Felesik, J., Vitello, L. B., and Erman, J. E. (2004) Azide binding to yeast cytochrome c peroxidase and horse metmyoglobin: comparative thermodynamic investigation using isothermal titration calorimetry, Arch. Biochem. Biophys. 422, 125-136.
37. Pierce, M. M., Raman, C. S., and Nall, B. T. (1999) Isothermal titration calorimetry of protein-protein interactions. Methods 19, 213-221.