Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells

Molecular Biology of the Cell

Volumn 8, Issue 8, 1997, Pages 1559-1573

  Eggers, Daryl K ^a   Welch, William J ^a   Hansen, William J ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CHAPERONE; CHAPERONIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; POLYPEPTIDE; TUBULIN;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; CROSS LINKING; CYTOSOL; HUMAN; HUMAN CELL; MAMMAL; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION;

ANIMALIA; MAMMALIA;

EID: 0030928059     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.8.8.1559     Document Type: Article

References (49)

1. Anfinsen, C.B. (1973). Principles that govern the folding of protein chains. Science 181, 223-230.
2. Beck, S.C., and De Maio, A. (1994). Stabilization of protein synthesis in thermotolerant cells during heat shock. J. Biol. Chem. 269, 21803-21811.
3. Becker, J., and Craig, E.A. (1994). Heat-shock proteins as molecular chaperones. Eur. J. Biochem. 219, 11-23.
4. Beckmann, R.P., Mizzen, L.A., and Welch, W.J. (1990). Interaction of hsp70 with newly synthesized proteins: implications for protein folding and assembly. Science 248, 850-854.
5. Blattler, D.P., Garner, F., Van Slyke, K., and Bradley, A. (1972). Quantitative electrophoresis in polyacrylamide gels of 2-40%. J. Chromatogr. 64, 147-155.
6. Brown, C.R., Martin, R.L., Hansen, W.J., Beckmann, R.P., and Welch, W.J. (1993). The constitutive and stress inducible forms of hsp70 exhibit functional similarities and interact with one another in an ATP-dependent fashion. J. Cell Biol. 120, 1101-1112.
7. Buchner, J. (1996). Supervising the fold: functional principles of molecular chaperones. FASEB J. 10, 10-19.
8. Dobrzynski, J.K., Sternlicht, M.L., Farr, G.W., and Sternlicht, H. (1996). Newly synthesized β-tubulin demonstrates domain-specific interactions with the cytosolic chaperonin. Biochemistry 35, 15870-15882.
9. Eggers, D.K. (1997). Characterization of nascent polypeptides and their molecular chaperones in mammalian cells. Ph.D. thesis, University of California, San Francisco.
10. Freeman, B.C., and Morimoto, R.I. (1996). The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. EMBO J. 15, 2969-2979.
11. Frydman, J., and Hartl, F.U. (1996). Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms. Science 272, 1497-1501.
12. Frydman, J., Nimmesgern, E., Erdjument-Bromage, H., Wall, J.S., Tempst, P., and Hartl, F.U. (1992). Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits. EMBO J. 11, 4767-4778.
13. Frydman, J., Nimmesgern, E., Ohtsuka, K., and Hartl, F.U. (1994). Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature 370, 111-117.
14. Georgopoulos, C., and Welch, W.J. (1993). Role of the major heat shock proteins as molecular chaperones. Annu. Rev. Cell Biol. 9, 601-634.
15. Gething, M.J., and Sambrook, J. (1992). Protein folding in the cell. Nature 355, 33-45.
16. Hansen, W.J., Lingappa, V.R., and Welch, W.J. (1994). Complex environment of nascent polypeptide chains. J. Biol. Chein. 269, 26610-26613.
17. Hartl, F.U. (1996). Molecular chaperones in cellular protein folding. Nature 381, 571-580.
18. Hendrick, J.P., and Hartl, F.U. (1995). The role of molecular chaperones in protein folding. FASEB J. 9, 1559-1569.
19. Hendrick, J.P., Langer, T., Davis, T.A., Hartl, F.U., and Wiedmann, M. (1993). Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides. Proc. Natl. Acad. Sci. USA 90, 10216-10220.
20. Hesterkamp, T., Hauser, S., Lutcke, H., and Bukau, B. (1996). E. coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. Proc. Natl. Acad. Sci. USA 93, 4437-4441.
21. Höhfeld, J., Minami, Y., and Hartl, F.U. (1995). Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle. Cell 83, 589-598.
22. Jakob, U., Lilie, H., Meyer, I., and Buchner, J. (1995). Transient interaction of hsp90 with early unfolding intermediates of citrate synthase. J. Biol. Chem. 270, 7288-7294.
23. Joly, E.C., Tremblay, E., Tanguay, R.M., Wu, Y., and Bibor-Hardy, V. (1994). TRiC-P5, a novel TCP1-related protein, is localized in the cytoplasm and in the nuclear matrix. J. Cell Science 107, 2851-2859.
24. Kubota, H., Hynes, G., and Willison, K. (1995). The chaperonin containing t-complex polypeptide 1 (TCP-1). Eur. J. Biochem. 230, 3-16.
25. Kudlicki, W., Odom, O.W., Kramer, G., and Hardesty, B. (1994). Chaperone-dependent folding and activation of ribosome-bound nascent rhodanese. J. Mol. Biol. 244, 319-331.
26. Lai, B.-T., Chin, N.W., Stanek, A.E., Keh, W., and Lanks, K.W. (1984). Quantitation and intracellular localization of the 85K heat shock protein by using monoclonal and polyclonal antibodies. Mol. Cell. Biol. 4, 2802-2810.
27. Langer, T., Lu, C., Echols, H., Flanagan, J., Hayer, M.K., and Hartl, F.U. (1992). Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature 356, 683-689.
28. Lewis, S.A., Tian, G., Vainberg, I.E., and Cowan, N.J. (1996). Chaperonin-mediated folding of actin and tubulin. J. Cell Biol. 132, 1-4.
29. Lewis, V.A., Hynes, G.M., Zheng, D., Saibil, H., and Willison, K. (1992). T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol. Nature 358, 249-252.
30. Lingappa, J.R., Martin, R.L., Wong, M.L., Ganem, D., Welch, W.J., and Lingappa, V.R. (1994). A eukaryotic cytosolic chaperonin is associated with a high molecular weight intermediate in the assembly of hepatitis B virus capsid, a multimeric particle. J. Cell Biol. 125, 99-111.
31. McCarty, J.S., Buchberger, A., Reinstein, J., and Bukau, B. (1995). The role of ATP in the functional cycle of DnaK chaperone system. J. Mol. Biol. 249, 126-137.
32. Milarski, K.L., Welch, W.J., and Morimoto, R.I. (1989). Cell cycle-dependent association of hsp70 with specific cellular proteins. J. Cell Biol. 108, 413-423.
33. Nelson, R.J., Ziegel hoffer, T., Nicolet, C., Werner-Washburne, M., and Craig, E.A. (1992). The translation machinery and 70 kD heat shock protein cooperate in protein synthesis. Cell 71, 97-105.
34. Ohtsuka, K. (1993). Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ. Biochem. Biophys. Res. Commun. 197, 235-240.
35. Palleros, D.R., Welch, W.J., and Fink, A.L. (1991). Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding. Proc. Natl. Acad. Sci. USA 88, 5719-5723.
36. Prapapanich, V., Chen, S., Nair, S.C., Rimerman, R.A., and Smith, D.F. (1996). Molecular cloning of human p48, a transient component of progesterone receptor complexes and an hsp-70 binding protein. Mol. Endocrinol. 10, 420-431.
37. Reid, B.G., and Flynn, G.C. (1996). GroEL binds to and unfolds rhodanese posttranslationally. J. Biol. Chem. 271, 7212-7217.
38. Sadis, S., and Hightower, L.E. (1992). Unfolded proteins stimulate molecular chaperone hsc70 ATPase by accelerating ADP/ATP exchange. Biochemistry 31, 9406-9412.
39. Safiejko-Mroczka, B., and Bell, P.B. (1996). Bifunctional protein cross-linking reagents improve labeling of cytoskeletal proteins for qualitative and quantitative fluorescence microscopy. J. Histochem. Cytochem. 44, 641-656.
40. Schmid, D., Baici, A., Gehring, H., and Christen, P. (1994). Kinetics of molecular chaperone action. Science 263, 971-973.
41. Schröder, H., Langer, T., Hartl, F.U., and Bukau, B. (1993). DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12, 4137-4144.
42. Schumacher, R.J., Hurst, R., Sullivan, W.P., McMahon, N.J., Toft, D.O., and Matts, R.L. (1994). ATP-dependent chaperoning activity of reticulocyte lysate. J. Biol. Chem. 269, 9493-9499.
43. Sternlicht, H., Farr, G.W., Sternlicht, M.L., Driscoll, J.K., Willison, K., and Yaffe, M.B. (1993). The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo. Proc. Natl. Acad. Sci. USA 90, 9422-9426.
44. Szabo, A., Langer, T., Schröder, H., Flanagan, J., Bukau, B., and Hartl, F.U. (1994). The ATP hydrolysis-dependent reaction cycle of the E. coli hsp70 system: DnaK, DnaJ, and GrpE. Proc. Natl. Acad. Sci. USA 91, 10345-10349.
45. Theyssen, H., Schuster, H.P., Packschies, L., Bukau, B., and Reinstein, J. (1996). The second step of ATP binding to DnaK induces peptide release. J. Mol. Biol. 263, 657-670.
46. Tian, G., Huang, Y., Rommelaere, H., Vandekerckhove, J., Ampe, C., and Cowan, N.J. (1996). Pathway leading to correctly folded β-tubulin. Cell 86, 287-296.
47. Valent, Q.A., Kendall, D.A., High, S., Kusters, R., Oudega, B., and Luirink, J. (1995). Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides. EMBO J. 14, 5494-5505.
48. Wiedmann, B., Sakai, H., Davis, T.A., and Wiedmann, M. (1994). A protein complex required for signal-sequence-specific sorting and translocation. Nature 370, 434-440.
49. Willison, K., Lewis, V., Zuckerman, K.S., Cordell, J., Dean, C., Miller, K., Lyon, M.F., and Marsh, M. (1989). The t complex polypeptide 1 (TCP-1) is associated with the cytoplasmic aspect of Golgi membranes. Cell 57, 621-632.