MAP2 prevents protein aggregation and facilitates reactivation of unfolded enzymes: Implications for the chaperone-like activity of MAP2

European Journal of Biochemistry

Volumn 271, Issue 8, 2004, Pages 1488-1496

  Sarkar, Taradas ^a   Mitra, Gopa ^a   Gupta, Suvroma ^a   Manna, Tapas ^a   Poddar, Asim ^a   Panda, Dulal ^b   Das, Kali P ^a   Bhattacharyya, Bhabatarak ^a  

^a BOSE INSTITUTE   (India)

^b INDIAN INSTITUTE OF TECHNOLOGY BOMBAY   (India)

Author keywords

Aggregation; C termini; MTP; Refolding; Tubulin

Indexed keywords

ALCOHOL DEHYDROGENASE; CELLULOSE PHOSPHATE; CHAPERONE; DITHIOTHREITOL; INSULIN; MICROTUBULE ASSOCIATED PROTEIN 2; TUBULIN;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CHROMATOGRAPHY; ENZYME REACTIVATION; INHIBITION KINETICS; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PURIFICATION; TEMPERATURE DEPENDENCE;

ALCOHOL DEHYDROGENASE; AMINO ACID SEQUENCE; AMINO ACIDS, ACIDIC; ANIMALS; ENZYME ACTIVATION; GLUCOSIDASES; GOATS; INSULIN; L-LACTATE DEHYDROGENASE; MALATE DEHYDROGENASE; MICROTUBULE-ASSOCIATED PROTEINS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN RENATURATION; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROMETRY, FLUORESCENCE; TAU PROTEINS; TRYPSIN; TUBULIN;

GENETTA;

EID: 2142701464     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04053.x     Document Type: Article

References (42)

1. Dustin, P. (1978) Microtubules, pp. 340-389. Springer Verlag, New York.
2. Sloboda, R.D. (1980) The role of microtubules in cell structure and cell division. Am. Sci. 68, 290-298.
3. Drewes, G., Ebneth, A. & Mandelkow, E.M. (1998) MAPs, MARKs and microtubule dynamics. Trends Biochem. Sci. 8, 307-311.
4. Punch, D.L. & Angelastro, J.M. (1994) Microtubule dynamics: bioenergetics and control. Adv. Enzymol. Relat. Areas Mol. Biol. 69, 121-154.
5. Williams, R.C., Caplow, M. & McIntosh, J.R. (1986) Cytoskeleton: dynamic microtubule dynamics. Nature 324, 106-107.
6. Desai, A. & Mitchison, T.J. (1997) Microtubule polymerization dynamics. Annu. Rev. Cell. Dev. Biol. 13, 83-117.
7. Nogales, E (2001) Structural insight into microtubule function. Annu. Rev. Biophys. Biomol. Struct. 30, 397-420.
8. Guha, S., Manna, T.K., Das, K.P. & Bhattacharyya, B. (1998) Chaperone-like activity of tubulin. J. Biol. Chem. 273, 30077-30080.
9. Manna, T., Sarkar, T., Poddar, A., Roychowdhury, M., Das, K.P. & Bhattacharyya, B. (2001) Chaperone-like activity of tubulin: binding and reactivation of unfolded substrate enzymes. J. Biol. Chem. 276, 39742-39747.
10. Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A.L. & Hartl, F. U. (1991) Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature 352, 36-42.
11. Das, K.P. & Surewicz, W.K. (1995) Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin. FEBS Lett. 369, 321-325.
12. Braig, K., Otwinowski, Z., Hegde, R., Boisvert, D.C., Joachimiak, A., Horwich, A.L. & Sigler, P.B. (1994) The crystal structure of the bacterial chaperonin GroEL at 2.8 Å. Nature 371, 578-586.
13. Andley, U.P., Mathur, S., Griest, T.A. & Petrash, J.M. (1996) Cloning, expression, and chaperone-like activity of human alphaA-crystallin. J. Biol. Chem. 271, 31973-31980.
14. Prasad, A.R.S., Luduena, R.F. & Horowitz, P.M. (1986) 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.
15. Ward, L.D. & Timasheff, S.N. (1994) Energy transfer studies of the distances between the colchicine, ruthenium red, and bisANS binding sites on calf brain tubulin. Biochemistry 33, 11891-11899.
16. Sarkar, N., Mukhopadhyay, K., Parrack, P.K. & Bhattacharyya, B. (1995) Aging of tubulin monomers using 5,5′-bis(8-anilino-1- naphthalenesulfonate) as a probe. Biochemistry 34, 13367-13373.
17. Chakraborty, S., Sarkar, N. & Bhattacharyya, B. (1999) Nucleotide-dependent bisANS binding to tubulin. Biochim. Biophys. Acta. 1432, 350-355.
18. Gupta, S., Chakraborty, S, Poddar, A., Sarkar, N., Das, K.P. & Bhattacharyya, B. (2003) BisANS binding to tubulin: isothermal titration calorimetry and the site-specific proteolysis reveal the GTP-induced structural stability of tubulin. Proteins Struct. Funct. Genet. 50, 283-289.
19. Sarkar, T., Manna, T., Bhattacharyya, S., Mahapatra, P., Poddar, A., Roy, S., Pena, J., Solana, R., Tarazona, R. & Bhattacharyya, B. (2001) Role of the carboxy-termini of tubulin on its chaperone-like activity. Proteins Struct. Funct. Genet. 44, 262-269.
20. Sloboda, R.D., Rudolph, S.A., Rosenbaum, J.L. & Greengard, P. (1975) Cyclic AMP-dependent endogenous phosphorylation of a microtubule-associated protein. Proc. Natl Acad. Sci. USA 72, 177-181.
21. Hamel, E. & Lin, C. (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.
22. Herzog, W. & Weber, K. (1978) Fractionation of brain microtubule-associated proteins: isolation of two different proteins which stimulate tubulin polymerization in vitro. Eur. J. Biochem. 92, 1-8.
23. 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.
24. Gamblin, T.C., Nachmanoff, K., Halpain, S. & Williams, R.C. Jr (1996) Recombinant microtubule-associated protein 2c reduces the dynamic instability of individual microtubules. Biochemistry 35, 12576-12586.
25. Kosik, K.S., Orecchio, L.D., Bakalis, S. & Neve, R.L. (1989) Developmentally regulated expression of specific tau sequences. Neuron 2, 1389-1397.
26. Panda, D., Goode, B.L., Feinstein, S.C. & Wilson, L. (1995) Kinetic stabilization of microtubule dynamics at steady state by tau and microtubule-binding domains of tau. Biochemistry 34, 11117-11127.
27. Bhattacharyya, B., Sackett, D.L. & Wolff, J. (1985) Tubulin, hybrid dimers, and tubulin S: stepwise charge reduction and polymerization. J. Biol. Chem. 260, 10208-10216.
28. Sackett, D.L., Bhattacharyya, B. & Wolff, J. (1985) Tubulin subunit carboxyl termini determine polymerization efficiency. J. Biol. Chem. 260, 43-45.
29. Chattopadhyay, S., Das, B., Bera, A.K., Dasgupta, D. & Dasgupta, C. (1994) Refolding of denatured lactate dehydrogenase by Escherichia coli ribosomes. Biochem. J. 300, 717-721.
30. Kopetzki, E., Schumacher, G. & Buckel, P. (1989) Control of formation of active soluble or inactive insoluble baker's yeast alpha-glucosidase PI in Escherichia coli by induction and growth conditions. Mol. Gen. Genet. 216, 149-155.
31. Ranson, N.A., Dunster, N.J., Burston, S.G. & Clarke, A.R. (1995) Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds. J. Mol. Biol. 250, 581-586.
32. Biswas, A., Saha, S. & Das, K.P. (2002) Structural features of molecular chaperones: a possible miceller connection. J. Surf. Sci. Technol. 18, 1-24.
33. r microtubule-associated proteins: properties and functions. Biochem. J. 259, 1-12.
34. Fenton, W.A. & Horwich, A.L. (1997) GroEL-mediated protein folding. Protein Sci. 6, 743-760.
35. Martin, J. & Hartl, F.U. (1997) Chaperone-assisted protein folding. Curr. Opin. Struct. Biol. 7, 41-52.
36. Sigler, P.B., Xu, Z., Rye, H.S., Burston, S.G., Fenton, W.A. & Horwich, A.L. (1998) Structure and function in GroEL-mediated protein folding. Annu. Rev. Biochem. 67, 581-608.
37. Goedert, M., Wischik, C.M., Crowther, R.A., Walker, J.E. & Klug, A. (1988) Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau. Proc. Natl Acad. Sci. USA 85, 4051-4055.
38. Bhattacharyya, J. & Das, K.P. (1999) Molecular chaperone-like properties of an unfolded protein, alpha(s)-casein. J. Biol. Chem. 274, 15505-15509.
39. Ostrerova, N., Petrucelli, L., Farrer, M., Mehta, N., Choi, P., Hardy, J. & Wolozin, B. (1999) alpha-Synuclein shares physical and functional homology with 14-3-3 proteins. J. Neurosci. 19, 5782-5791.
40. Hendrick, J.P. & Hartl, F.U. (1993) Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem. 62, 349-384.
41. Gao, Y., Thomas, J.O., Chow, R.L., Lee, G.H. & Cowan, N.J. (1992) A cytoplasmic chaperonin that catalyzes beta-actin folding. Cell 69, 1043-1050.
42. Melki, R. & Cowan, N.J. (1994) Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates. Mol. Cell. Biol. 14, 2895-2904.