Analysis of tubulin oligomers by analytical ultracentrifugation

Methods in Cell Biology

Volumn 95, Issue C, 2010, Pages 274-288

  Correia, John J ^a  

^a UNIVERSITY OF MISSISSIPPI MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; TUBULIN; VINCA ALKALOID;

ANIMAL; CHEMISTRY; COMPUTER PROGRAM; DIAGNOSIS, MEASUREMENT AND ANALYSIS; DRUG EFFECT; HUMAN; IMAGE PROCESSING; MACROMOLECULE; METABOLISM; METHODOLOGY; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; REVIEW; ULTRACENTRIFUGATION;

ANIMALS; ANTINEOPLASTIC AGENTS; HUMANS; IMAGE PROCESSING, COMPUTER-ASSISTED; LABORATORY TECHNIQUES AND PROCEDURES; MACROMOLECULAR SUBSTANCES; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; SOFTWARE; TUBULIN; ULTRACENTRIFUGATION; VINCA ALKALOIDS;

EID: 77955289716     PISSN: 0091679X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0091-679X(10)95015-2     Document Type: Book

References (54)

1. Alday, P. H., and Correia, J. J. (2009). Macromolecular interaction of halichondrin B analogs Eribulin (E7389) and ER-076349 with tubulin by analytical ultracentrifugation. Biochemistry. 48, 7927-7938.
2. Alday, P. H. (2009). Use of Fluorescently Labeled Proteins in Quantitative Sedimentation Velocity Studies of Heterogeneous Biomolecular Interactions. Ph.D. Thesis, University of Mississippi Medical Center, Jackson, MS.
3. Bosch, M., Le, K. H., Bugyi, B., Correia, J. J., Renault, L., and Carlier,M.-F. (2007). Analysis of the function of Spire in actin assembly and its synergy with formin and profiline. Mol. Biol. Cell. 28, 555-568.
4. Casassa, E. F., and Eisenberg, H. (1964). Thermodynamic analysis of multicomponent solutions. Adv. Protein Chem. 19, 287-395.
5. Cochran, J. C., Sontag, C. A., Maliga, Z., Kapoor, T. M., Correia, J. J., and Gilbert, S. P. (2004). Mechanistic analysis of the mitotic kinesin Eg5. J. Biol. Chem. 269, 38861-38870.
6. Correia, J. J. (2000). The analysis of weight average sedimentation data. Meth. Enzymol. 321, 81-100.
7. Correia, J. J., Alday, P. H., Sherwood, P., and Stafford, W. F. (2009). Effect of kinetics on sedimentation velocity profiles and the role of intermediates. In "Numerical Methods" (M. L. Johnson, ed.), Vol. 467, 135-161.
8. Correia, J. J., Gilbert, S. P., Moyer, M. L., and Johnson, K. A. (1995). Sedimentation studies on the kinesin head domain constructs K401, K366 and K341. Biochemistry. 34, 4898-4907.
9. Correia, J. J., and Lobert, S. (2001). Physiochemical aspects of tubulin-interacting, antimitotic drugs. Curr. Pharm. Design. 7(13), 1213-1228.
10. Correia, J. J., and Lobert, S. (2008). Molecular mechanisms of micotubule acting cancer drugs. In "Microtubule Targets in Cancer Therapy" (A. T. Fojo, ed.), pp. 21-46. Humana Press, Totowa, NJ.
11. Correia, J. J., Sontag, C. A., Stafford,W. F., and Sherwood, P. J. (2005). Models for direct boundary fitting of indefinite ligand-linked self-association. In "Analytical Ultracentrifugation: Techniques and Methods" (D. Scott, S. Harding and A. Rowe, eds.), pp. 51-63. Springer, Berlin.
12. Correia, J. J., and Stafford,W. F. (2009). Extracting equilibrium constants from kinetically limited reacting systems. In "Biothermodynamics", Part A (M. L. Johnson, ed.), Vol 455, pp. 419-446. Academic Press, San Diego.
13. De Marco, V., de Marco, A., Correia, J. J., Goldie, K. N., and Hoenger, A. (2003). Dimerization properties of a Xenopus Laevis Kinesin-II C-terminal stalk fragment. EMBO Reports. 4, 717-722.
14. Desai, A., Verma, S., Mitchison, T. J., and Walczak, C. E. (1999). Kin I kinesins are microtubuledestabilizing enzymes. Cell. 99, 69-78.
15. Devred, F., Barbier, P., Douillard, S., Monasterio, O., Andreu, J. M., and Peyrot, V. (2004). Tau induces ring and microtubule formation from ab-Tubulin dimers under nonassembly conditions. Biochemistry. 43, 10520-10531.
16. Dönges, K. H., Biedert, S., and Paweletz, N. (1976). Characterization of a 20S component in tubulin from mammalian brain. Biochemistry. 15, 2995-2999.
17. Foster, K. A., Correia, J. J., and Gilbert, F. P. (1998). Equilibrium Binding Studies of Non-claret Disjunctional Protein (Ncd). J. Biol. Chem. 273, 35307-35318.
18. Frigon, R. P., and Timasheff, S. N. (1975a). Magnesium-induced self-association of calf brain tubulin. I. Stoichiometry. Biochemistry. 14, 4559-4566.
19. Frigon, R. P., and Timasheff, S. N. (1975b). Magnesium-induced self-association of calf brain tubulin. II. Thermodynamics. Biochemistry. 14, 4567-4573.
20. Howard, W. D., and Timasheff, S. N. (1986). GDP state of tubulin: Stabilization of double rings. Biochemistry. 25, 8292.
21. Jourdain, L., Curmi, P., Sobel, A., Pantaloni, D., and Carlier, M. F. (1997). Stathmin: A tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules. Biochemistry. 36, 10817-10821.
22. Jourdain, I., Lachkar, S., Charbaut, E., Gigant, B., Knossow, M., Sobel, A., and Curmi, P. A. (2004). A synergistic relationship between three regions of stathmin family proteins is required for the formation of a stable complex with tubulin. Biochem. J. 378, 877-888.
23. Kar, S. R., Kingsbury, J. S., Lewis, M. S., Laue, T. M., and Schuck, P. (2000). Analysis of transport experiments using pseudo-absorbance data. Anal. Biochem. 285, 135-142.
24. Kerssemakers, J. W., Munteanu, E. L., Laan, L., Noetzel, T. L., Janson, M. E., and Dogterom, M. (2006). Assembly dynamics of microtubules at molecular resolution. Nature. 442, 709-712.
25. Kirschner, M. W., Williams, R. C., Weingarten, M., and Gerhart, J. C. (1974). Microtubules from mamallian brain: Some properties of their depolymerization products and a proposed mechanism of assembly and disassembly. PNAS. 71, 1159-1163.
26. Liu, S., and Stafford, W. F. (1995). An optical thermometer for direct measurement of cell temperature in the Beckman instruments XL-A analytical ultracentrifuge. Anal. Biochem. 224, 199-202.
27. Lobert, S., Boyd, C. A., and Correia, J. J. (1997). Divalent cation and ionic strength effects on vinca alkaloid-induced tubulin self-association. Biophys. J. 72, 416-427.
28. Lobert, S., and Correia, J. J. (2000). Energetics of vinca alkaloid interactions with tubulin. Meth. Enzymol. 323, 77-103.
29. Lobert, S., and Correia, J. J. (2007). Methods for studying vinca alkaloid interaction with tubulin. In "Microtubule Protocols" (J. Zhou, ed.), pp. 261-280, Chapter 18. Humana Press, Totowa, NJ.
30. Lobert, S., Fahy, J., Hill, B. T., Duflos, A., Entievant, C., and Correia, J. J. (2000). Vinca alkaloid-induced tubulin spiral formation correlates with cytotoxicity in the leukemic L1210 cell line. Biochemistry. 39, 12053-12062.
31. Lobert, S., Frankfurter, A., and Correia, J. J. (1995). Binding of vinblastine to phosphocellulose-purified and αβ-Class III tubulin: The role of nucleotides and β-tubulin isotypes. Biochemistry. 34, 8050-8060.
32. Lobert, S., Frankfurter, A., and Correia, J. J. (1998a). The energetics of vinca alkaloid interactions with β-tubulin isotypes: Implications for drug efficacy and toxicity. Cell Motil. Cytoskel. 39, 107-121.
33. Lobert, S., Ingram, J. W., and Correia, J. J. (2007). The thermodynamics of vinca alkaloid-induced tubulin spiral formation. Biophys. Chem., Special Issue, Festschrift for Julian Sturtevant. 126.
34. Lobert, S., Ingram, J. W., Hill, B. T., and Correia, J. J. (1998b). A comparison of thermodynamic parameters for vinorelbine- and vinflunine-induced tubulin self association by sedimentation velocity. Mol. Pharmacol. 53, 908-915.
35. Lobert, S., Vulevic, B., and Correia, J. J. (1996). Interaction of vinca alkaloids with tubulin: A comparison of vinblastine, vincristine and vinorelbine. Biochemistry. 35, 6806-6814.
36. MacGregor, I. K., Anderson, A. L., and Laue, T. M. (2004). Fluorescence detection for the XLI ultracentrifuge. Biophys. Chem. 108, 165-185.
37. Mackey, A. T., Sontag, C. A., Satterwhite, L. L., Correia, J. J., and Gilbert, S. P. (2004). The ATPase mechanism behind the microtubule-based motility of GST-Kar3. J. Biol. Chem. 279, 51354-51361.
38. Marcum, J. M., and Borisy, G. G. (1978a). Sedimentation velocity analyses of the effect of hydrostatic pressure on the 30 S microtubule protein oligomer. J. Biol. Chem. 253(8), 2852-2857.
39. Marcum, J. M., and Borisy, G. G. (1978b). Characterization of microtubule protein oligomers by analytical ultracentrifugation. J. Biol. Chem. 253(8), 2825-2833.
40. Na, G. C., and Timasheff, S. N. (1980). Stoichiometry of the vinblastine-induced self-association of calf brain tubulin. Biochemistry. 19, 1347-1354.
41. Na, G. C., and Timasheff, S. N. (1986). Interaction of vinblastine with calf brain tubulin: Effects of magnesium ions. Biochemistry. 25, 6222-6228.
42. O'Brien, E. T., Salmon, E. D., Walker, R. A., and Erickson, H. P. (1990). The effects of magnesium on dynamic instability of individual microtubules. Biochemistry. 29, 6648-6656.
43. Penefsky, H. S. (1979). A centrifuged-column procedure for the measurement of ligand binding by beef heart F1. Methods Enzymol. 56, 527-531.
44. Rosenfeld, S. S., Correia, J. J., Xing, J., Rener, B., and Cheung, H. C. (1996b). Structural studies of kinesin-nucleotide intermediates. J. Biol. Chem. 271, 30212-30221.
45. Rosenfeld, S. S., Rener, B., Correia, J. J., Mayo, M. S., and Cheung, H. C. (1996a). Equilibrium studies of kinesin: Nucleotide intermediates. J. Biol. Chem. 271, 9473-9482.
46. Rosenfeld, S. S., Van Duffelen, M., Behnke Parks, W. M., Beadle, C., Corrreia, J. J., and Xing, J. (2009). THE ATPase cycle of the mitotic motor CENP-E. J. Biol. Chem. 284, 32858-32868.
47. Scheele, R. B., and Borisy, G. G. (1978). Electron microscopy of metal-shadowed and negatively stained microtubule protein. Structure of the 30 S oligomer. J. Biol. Chem. 253, 2846-2851.
48. Schuck, P. (2000). Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78, 1606-1619.
49. Sontag, C. A., Stafford, W. F., and Correia, J. J. (2004). A comparison of weight average and direct boundary fitting of sedimentation velocity data for indefinite polymerizing systems. Biophys. Chem. 108, 215-230.
50. Stafford, W. F. (1992). Boundary analysis in sedimentation transport experiments: A procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile. Anal. Biochem. 203, 295-301.
51. Stafford, W. F. (2009). Protein-protein and ligand-protein interactions studied by analytical ultracentrifugation. In "Protein Structure, Stability, and Interactions" (J. W. Shriver, ed.), Vol. 490, pp. 83-113. Humana Press, Totowa NJ.
52. Stafford,W. F., and Sherwood, P. J. (2004). Analysis of heterologous interacting systems by sedimentation velocity: Curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and rate constants. Biophys. Chem. 108, 231-243.
53. Vallee, R. B., and Borisy, G. G. (1978). The non-tubulin component of microtubule protein oligomers. Effect on self-association and hydrodynamic properties. J. Biol. Chem. 253(8), 2834-2845.
54. Vulevic, B., Lobert, S., and Correia, J. J. (1997). Role of guanine nucleotides in the vinca alkaloid-induced self association of tubulin: Effects of GMPCPP and GMPCP. Biochemistry. 36, 12828-12835.