Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors

Journal of Cell Biology

Volumn 138, Issue 4, 1997, Pages 821-832

  Tian, Guoling ^a   Lewis, Sally A ^a   Feierbach, Becket ^b   Stearns, Timothy ^b   Rommelaere, Heidi ^c   Ampe, Christophe ^c   Cowan, Nicholas J ^a  

^a NEW YORK UNIVERSITY MEDICAL CENTER   (United States)

^b STANFORD UNIVERSITY   (United States)

^c DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TUBULIN; BETA TUBULIN; CHAPERONIN; GUANOSINE TRIPHOSPHATE;

ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING;

AMINO ACID SEQUENCE; ANIMALS; CATTLE; CHAPERONINS; DIMERIZATION; DNA-BINDING PROTEINS; GUANOSINE TRIPHOSPHATE; HYDROLYSIS; MICROTUBULE-ASSOCIATED PROTEINS; MOLECULAR SEQUENCE DATA; NEOPLASM PROTEINS; PROTEIN CONFORMATION; PROTEIN FOLDING; RABBITS; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY, AMINO ACID; TRANSCRIPTION FACTORS; TUBULIN;

EID: 0030820735     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.138.4.821     Document Type: Article

References (38)

1. Amberg, D.C., D. Botstein, and E.M. Beasley. 1996. Precise gene disruption in Saccharomyces cerevisiae by double fusion polymerase chain reaction. Yeast. 11:1275-1280.
2. Anfinsen, C.B. 1973. Principles that govern the folding of protein chains. Science. (Wash. DC). 181:223-230.
3. Archer, J.E., L.R. Vega, and F. Solomon. 1995. Rbl2, a yeast protein that binds to β-tubulin and participates in microtubule function in vivo. Cell. 82:425-434.
4. Baldwin, T.O., M.M. Ziegler, A.F. Chaffotte, and M.E. Goldberg. 1993. Contribution of folding steps involving the individual subunits of bacterial luciferase to the assembly of the active heterodimeric enzyme. J. Biol. Chem. 268:10766-10772.
5. Bhattacharyya, B., D.L. Sackett, and J. Wolff. 1985. Tubulin, hybrid dimers, and tubulin S. J. Biol. Chem. 260:10208-10216.
6. Chen, X., D.S. Sullivan, and T. Huffaker. 1994. Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo. Proc. Natl. Acad. Sci. USA. 91:9111-9115.
7. Clark, A.C., J.F. Sinclair, and T.L. Baldwin. 1993. Folding of bacterial luciferase involves a non-native heterodimeric intermediate in equilibrium with native enzyme and the unfolded subunits. J. Biol. Chem. 268:10773-10779.
8. Detrich, H.W., III, and R.C. Williams. 1978. Reversible dissociation of the alpha beta dimer of tubulin from bovine brain. Biochemistry. 17:3900-3907.
9. Eriksson, S., I.W. Caras, and D.W. Martin. 1982. Direct photoaffinity labeling of an allosteric site on subunit protein M1 of mouse ribonucleotide reductase bv dTTP. Proc. Natl. Acad. Sci. USA. 79:81-85.
10. Fontabla, A., R. Paciucci, J. Avila, and J.C. Zabala. 1993. Incorporation of tubulin subunits into dimers requires GTP hydrolysis. J. Cell Sci. 106:627-632.
11. Frydman, J., E. Nimmesgern, H. Erdjument-Bromage, J.S. Wall, P. Tempst, and F-U. Hartl. 1992. Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits. EMBO (Eur. Mol. Biol. Organ.) J. 11:4767-4778.
12. Gao, Y., J.O. Thomas, R.L. Chow, G-H. Lee, and N.J. Cowan. 1992. A cytoplasmic chaperonin that catalyzes β-actin folding. Cell. 69:1043-1050.
13. Gao, Y., I.E., Vainberg, R.L. Chow, and N.J. Cowan. 1993. Two cofactors and cytoplasmic chaperonin are required for the folding of α-and β-tubulin. Mol. Cell. Biol. 13:2478-2485.
14. Gao, Y., R. Melki, P. Walden, S.A. Lewis, C. Ampe, H. Rommelaere, J. Vandekerckhove, and N.J. Cowan. 1994. A novel cochaperonin that modulates the ATPase activity of cytoplasmic chaperonin. J. Cell Biol. 125:989-996.
15. Hartl, F-U. 1996. Molecular chaperones in cellular protein folding. Nature (Lond.). 381:571-580.
16. Horwich, A.L., J.S. Weissman, and W.A. Fenton. 1995. Kinesis of polypeptide during GroEL-mediated folding. Cold Spring Harbor Symp. Quant. Biol. 60: 435-440.
17. Hoyt, M.A., T. Stearns, and D. Botstein. 1990. Chromosome instability mutants of Saccharomyces cerevisiae that are defective in microtubule-mediated processes. Mol. Cell. Biol. 10:223-234.
18. Hoyt, M.A., J.P. Macke, B.T. Roberts, and J.R. Geiser. 1997. Saccharomyces cerevisiae PAC2 functions with CIN1, 2 and 4 in a pathway leading to normal microtubule stability. Genetics. 146:849-857.
19. Ito, H., Y. Fukada, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163-168.
20. Lewis, S.A., G. Tian, I.E., Vainberg, and N.J. Cowan. 1996. Chaperonin-mediated folding of actin and tubulin. J. Cell Biol. 132:1-4.
21. Marschall, L., R. Jeng, J. Mulholland, and T. Stearns. 1996. Analysis of Tub4p, a yeast γ-tubulin-like protein: implications for microtubule organizing center function. J. Cell Biol. 134:443-454.
22. Melki, R., I.E., Vainberg, R.L. Chow, and N.J. Cowan. 1993. Chaperonin-mediated folding of vertebrate actin-related protein and γ-tubulin. J. Cell Biol. 122:1301-1310.
23. Melki, R., H. Rommelaere, R. Leguy, J. Vandekerckhove, and C. Ampe. 1996. Cofactor A is a molecular chaperone required for β-tubulin folding: functional and structural characterization. Biochemistry. 35:10422-10435.
24. Mitchison, T., and M.W. Kirschner. 1986. Beyond self-assembly: from microtubules to morphogenesis. Cell. 45:329-342.
25. Murphy, D.B., R.B. Vallee, and G.G. Borisy. 1977. Identity and polymerization-stimulatory activity of the non-tubulin proteins associated with microtubules. Biochemistry. 16:2598-2606.
26. Paciucci, R. 1994. Role of 300kD complexes as intermediates in tubulin folding and dimerization: characterization of a 25kD cytosolic protein involved in the GTP-dependent release of monomeric tubulin. Biochem. J. 301:105-110.
27. Pierre, P., J. Scheel, J.E. Rickard, and T. Kreis. 1992. CLIP-170 links endocytic vesicles to microtubules. Cell. 70:887-900.
28. Sackett, D., B. Bhattacharyya, and J. Wolff. 1985. Tubulin subunit carboxyl termini determine polymerization efficiency. J. Biol. Chem. 260:43-45.
29. Sherman, F., G.R. Fink, and J.B. Hicks. 1983. Methods in Yeast Genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
30. Sikorski, R.S., and P. Hieter. 1989. A study of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics. 122:19-27.
31. Spiegelman, B.M., S.M. Penningroth, and M.W. Kirschner. 1977. Turnover of tubulin and the N-site GTP in Chinese hamster ovary cells. Cell. 12:587-600.
32. Stearns, T., M.A. Hoyt, and D. Botstein. 1990. Yeast mutants sensitive to antimicrotubule drugs define three genes that affect microtubule function. Genetics. 124:251-262.
33. Tian, G., I.E., Vainberg, W.D. Tap, S.A. Lewis, and N.J. Cowan. 1995a. Specificity in chaperonin-mediated protein folding. Nature (Lond.). 375:250-253.
34. Tian, G., I.E., Vainberg, W.D. Tap, S.A. Lewis, and N.J. Cowan. 1995b. Quasinative chaperonin-bound intermediates in facilitated protein folding. J. Biol. Chem. 270:23910-23913.
35. Tian, G., Y. Huang, H. Rommelaere, J. Vandekerckhove, C. Ampe, and N.J. Cowan. 1996. Pathway leading to correctly folded β-tubulin. Cell. 86:287-296.
36. Ursic, D., J.C. Sedbrook, K.L. Himmel, and M.R. Culbertson. 1994. The essential yeast TCP1 protein affects actin and microtubules. Mol. Biol. Cell. 5:1065-1080.
37. Vinh, D., and D.G. Drubin. 1994. A yeast TCP-1-like protein is required for actin formation in vivo. Proc. Natl. Acad. Sci. USA. 91:9116-9120.
38. Zabala, J.C., and N.J. Cowan. 1992. Tubulin dimer formation via the release of α-and β-tubulin monomers from multimolecular complexes. Cell Motil. Cytoskeleton. 23:222-230.