Sulfhydryls of tubulin: A probe to detect conformational changes of tubulin

European Journal of Biochemistry

Volumn 267, Issue 12, 2000, Pages 3469-3476

  Roychowdhury, Manami ^a   Sarkar, Nabanita ^a   Manna, Tapas ^a   Bhattacharyya, Shankar ^a   Sarkar, Taradas ^a   BasuSarkar, Pampi ^a   Roy, Siddhartha ^a   Bhattacharyya, Bhabatarak ^a  

^a BOSE INSTITUTE   (India)

Author keywords

Ageing; Colchicine; Cysteine; DTNB; Tubulin

Indexed keywords

TUBULIN;

AGING; AMINO ACID SEQUENCE; ARTICLE; CONFORMATIONAL TRANSITION; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN CONFORMATION;

ANILINO NAPHTHALENESULFONATES; ANIMALS; COLCHICINE; CYSTEINE; DITHIONITROBENZOIC ACID; PROTEIN CONFORMATION; RABBITS; SULFHYDRYL COMPOUNDS; SULFHYDRYL REAGENTS; TIME FACTORS; TROPOLONE; TUBULIN;

EID: 0033920014     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01369.x     Document Type: Article

References (26)

1. 1. Krauhs, E., Little, M., Kempf, T., Hofer-Warbinek, R. & Ade, W. & Ponstingl, H. (1981) Complete amino acid sequence of beta-tubulin from porcine brain. Proc. Natl Acad. Sci. USA 78, 4156-4160.
2. 2. Ponstingl, H., Krauhs, E. & Little, M. & Kempf. T. (1981) Complete amino acid sequence of alpha-tubulin from porcine brain. Proc. Natl Acad. Sci. USA 78, 2757-2761.
3. 3. Nogales, E. & Wolf, S.G. & Downing, K.H. (1998) Structure of the αβ tubulin dimer by electron crystallography. Nature 391, 199-203.
4. 4. Little, M. & Luduena, R.F. (1985) Structural differences between brain beta1-and beta2-tubulins: implications for microtubule assembly and colchicine binding. EMBO J. 4, 51-56.
5. 5. Little, M. & Luduena, R.F. (1987) Location of two cysteines in brain beta1-tubulin that can be cross-linked after removal of exchangeable GTP. Biochem. Biophys. Acta 912, 28-33.
6. 6. Hamel, E. & Lin, L. (1981) Glutamate-induced polymerization of tubulin: characteristics of the reaction and application to the large-scale purification of tubulin. Arch. Biochem. Biophys. 209, 29-40.
7. 7. Lowry, O.H., Rosenbrough, N.J. & Farr, A.L. & Randall, R.J. (1951) Protein measurement with the folin phenol reagent. J. Biol. Chem. 193, 265-275.
8. 8. Weisenberg, R.C. & Borisy, G.G. & Taylor, E.W. (1968) The colchicine binding protein of mammalian brain and its relation to microtubules. Biochemistry 7, 4466-4479.
9. 9. Ellman, G.L. (1959) Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82, 70-77.
10. 10. Pyles, E.A. & Bane Hastie, S. (1993) Effect of the B-ring and the C-7 substituent on the kinetics of colchicinoid-tubulin associations. Biochemistry 32, 2329-2336.
11. 11. Haugland, R.P. (1994) Handbook of Fluorescent Probes & Research Chemicals, 5th edn. Molecular Probes Inc., Eugene, OR, USA.
12. 12. Hamel, E. (1990) Interactions of tubulin with small ligands. In Microtubule Proteins (Avila, J. ed.), pp. 89-191. CRC Press, Boca Raton, FL.
13. 13. Sackett, D.L. & Verma, J.K. (1993) Molecular mechanism of colchicine action: induced local unfolding of β-tubulin. Biochemistry 32, 13560-13565.
14. 14. Basusarkar, P. & Chandra, S. & Bhattacharyya, B. (1997) The colchicine-binding and pyrene-excimer-formation activities of tubulin involve a common cysteine residue in the beta subunit. Eur. J. Biochem. 244, 378-383.
15. 15. Chakraborti, G. & Sengupta, S. & Bhattacharyya, B. (1996) Thermodynamics of cochicinoid-tubulin interactions. Role of B-ring and C-7 substituent. J. Biol. Chem. 271, 2897-2901.
16. 16. Banerjee, S. & Chakraborti, G. & Bhattacharyya, B. (1997) Colchicine binding to tubulin monomers: a mechanistic study. Biochemistry 36, 5600-5606.
17. 17. Hilton, B.D. & Woodward, C.K. (1979) On the mechanism of istope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor. Biochemistry 18, 5834-5841.
18. 18. Woodward, C.K. & Hilton, B.D. (1979) Hydrogen exchange kinetics and internal motions in proteins and nucleic acids. Annu. Rev. Biophys. Bioeng. 8, 99-127.
19. 19. Lee, J.C., Corfman, D. & Frigon, R.P. & Timasheff, S.N. (1978) Conformational study of calf brain tubulin. Arch. Biochem. Biophys. 185, 4-14.
20. 6 glial cell microtubule protein decays much faster than its colchicine-binding activity. Nature 269, 435-436.
21. 21. Prasad, A.R.S. & Luduena, R.F. & Horowitz, P.M. (1986b) Detection of energy transfer between tryptophan residues in the tubulin molecule and bound bis (8-anilinonaphthalene-1-sulfonate), an inhibitor of microtubule assembly, that binds to a flexible region on tubulin. Biochemistry 25, 3536-3540.
22. 22. Ward, L.D. & Timasheff, S.N. (1994) Cooperative multiple binding of bisANS and daunomycin to tubulin. Biochemistry 33, 11891-11899.
23. 23. Sarkar, N., Mukhopadhyay, K. & Parrack, P.K. & Bhattacharyya, B. (1995) Aging of tubulin monomers using 5,5′-bis (8-anilino-1-naphthalene sulfonate) as a probe. Biochemistry 34, 13367-13373.
24. 24. Wilson, L. (1970) Properties of colchicine binding protein from chick embryo brain. Interactions with vinca alkaloids and podophyllotoxin. Biochemistry 9, 4999-5007.
25. 25. Lee, B. & Richards, F.M. (1971) The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55, 379-400.
26. 26. Fraczkiewicz, R. & Braun, W. (1998) Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules. J. Comp. Chem. 19, 319-333.