Protein self-organization in vitro and in vivo: Partitioning between physical biochemistry and cell biology

Biological Chemistry

Volumn 379, Issue 3, 1998, Pages 237-243

  Jaenicke, Rainer ^a  

^a UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

Aggregation; Association; Chaperones; Folding; In vitro; In vivo

Indexed keywords

CHAPERONE; PROTEIN; SOLVENT;

BIOCHEMISTRY; KINETICS; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; REVIEW;

MOLECULAR CHAPERONES; PROTEIN FOLDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; SOLVENTS;

EID: 0031923551     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

References (51)

1. Ansari, A., Berendzen, J., Browne, S.F., Frauenfelder, H., Iben, I.E.T., Sauke, T.B., Shyamsunder, E., and Young, R.D. (1985). Protein states and protein quakes. Proc. Natl. Acad. Sci. USA 82, 5000-5004.
2. Baldwin, R.L. (1995). The nature of protein folding pathways. J. Biomol. NMR 5, 103-109.
3. Baldwin, R.L. (1996). On-pathway vs off-pathway folding intermediates. Fold. Des. 1, R1-8.
4. Bergman, L.W., and Kuehl, W.M. (1979). Co-translational modification of nascent immunoglobulin heavy and light chains. J. Supramol. Struct. 11, 9-24.
5. Branden, C., and Tooze, J. (1991). Introduction to Protein Structure. (New York, London: Garland Publ.) 302 pp.
6. Buchner, J., and Rudolph, R. (1991). Routes to active proteins. Curr. Opin. Biotech. 2, 532-538.
7. Creighton, T.E., ed. (1992). Protein Folding. (New York: Freeman) p. 547.
8. Danner, M., and Seckler, R. (1993). Mechanism of phage P22 tail-spike protein folding mutations. Protein Sci. 2, 1869-1881.
9. Eaton, W.A., Muñoz, V., Thompson, P.A., Chan, C.-K., and Hofrichter, J. (1997). Submillisecond kinetics of protein folding. Curr. Opin. Struct. Biol. 7, 10-14.
10. Fersht, A.R. (1997). Nucleation mechanisms in protein folding. Curr. Opin. Struct. Biol. 7, 3-9.
11. Fink, A.L., and Goto, Y., eds. (1997). Molecular Chaperones in the Life Cycle of Proteins. (New York: M. Dekker) 626 pp.
12. Freedman, R.B. (1992). Protein folding in the cell. In: Protein Folding, Creighton, I.E., ed. (New York: Freeman), pp. 455-539.
13. Gerl, M., Rudolph, R., and Jaenicke, R. (1985). Mechanism and specificity of reconstitution of dimeric LDH from Limulus polyphemus. Biol. Chem. Hoppe Seyler 366, 447-454.
14. Goldberg, M.E., Rudolph, R., and Jaenicke, R. (1991). A kinetic study of the competition between renaturation and aggregation during the refolding and denatured-reduced egg-white lysozyme. Biochemistry 30, 2790-2797.
15. Groß, M., and Jaenicke, R. (1994). Proteins under pressure: The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes. Eur. J. Biochem. 221, 617-630.
16. Hecht, K., and Jaenicke, R. (1989). MDH from the extreme halophilic archaeon Halobacterium marismortui: Reconstitution of the enzyme after denaturation and dissociation in various denaturants. Biochemistry 28, 4979-4985.
17. Helenius, A., Marquardt, T., and Braakman, I. (1992). The ER as a protein-folding compartment. Trends Cell Biol. 2, 227-231.
18. Herbst, R., Schaefer, U., and Seckler, R. (1997). Equilibrium intermediates in the reversible unfolding of firefly luciferase. J. Biol. Chem. 272, 7099-7105.
19. Hirs, C.H.W., and Timasheff, S.N., eds. (1986). Enzyme Structure, Part L. Meth. Enzymol. 131, 3-280.
20. Jaenicke, R. (1981). Enzymes under extremes of physical conditions. Annu. Rev. Biophys. Bioeng. 10, 1-67.
21. Jaenicke, R. (1987). Folding and association of proteins. Prog. Biophys. Mol. Biol. 49, 117-237.
22. Jaenicke, R. (1991). Protein stability and molecular adaptation to extreme conditions. Eur. J. Biochem. 202, 715-728.
23. Jaenicke, R. (1996). Protein Folding and Association: In vitro studies for self-organization and targeting in the cell. Curr. Top. Cell. Reg. 34, 209-314.
24. Jaenicke, R., and Perham, R.N. (1982). Reconstitution of the PDH multienzyme complex from B. stearothermophilus. Biochemistry 21, 3378-3385.
25. Jaenicke, R., Schurig, H., Beaucamp, N., and Ostendorp, R. (1996). Structure and stability of hyperstable proteins: Glycolytic enzymes from Thermotoga maritima. Adv. Protein Chem. 48, 181-269.
26. Kiefhaber, T., Rudolph, R., Kohler, H.-H., and Buchner, J. (1991). Protein aggregation in vitro and in vivo. Bio/Technology 9, 825-829.
27. Kim, P.S., and Baldwin, R.L. (1990). Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59, 631-660.
28. Kolb, V.A., Makeyev, E.V., and Spirin, A.S. (1994). Folding of firefly luciferase during translation in cell-free system. EMBO J. 13, 3631-3637.
29. Komar, A.A., and Jaenicke, R. (1995). Kinetics of translation of γ-crystallin and its circularly permuted variant in an in vitro cell-free system: Possible relations to codon distribution and protein folding. FEBS Lett. 376, 195-198.
30. Komar, A.A., Kommer, A., Krasheninnikov, I.A., and Spirin, A.S. (1997). Cotranslational folding of globin. J. Biol. Chem. 272, 10646-10651.
31. Lehle, K., Wrba, A., and Jaenicke, R. (1994). Erythrina caffra trypsin inhibitor retains its native structure and function after reducing its disulfide bonds. J. Mol. Biol. 239, 276-284.
32. Mayr, E.-M., Jaenicke, R., and Glockshuber, R. (1997). The domains in γB-crystallin: Identical fold - different stabilities. J. Mol. Biol. 269, 260-269.
33. Muñoz, V., Thompson, P.A., Hofrichter, J., and Eaton, W.A. (1997). Folding dynamics and mechanism of β-hairpin formation. Nature 390, 196-199.
34. Opitz, U., Rudolph, R., Jaenicke, R., Ericsson, L., and Neurath, H. (1987). Proteolytic dimers of porcine muscle LDH: Characterization, folding and reconstitution of the truncated and nicked polypeptide chain. Biochemistry 26, 1399-1406.
35. Pelham, H.R.B. (1989). Control of protein exit from the ER. Annu. Rev. Cell Biol. 5, 1-23.
36. Peng, Z.-Y., and Kim, P.S. (1994). A protein dissection study of a molten globule. Biochemistry 33, 2136-2141.
37. Perl, D., Welker, C., Schindler, T., Schröder, K., Marahiel, M.A., Jaenicke, R., and Schmid, F.X. (1998). Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nature Struct. Biol., in press.
38. Peters, T., Jr., and Davidson, L.K. (1982). The biosynthesis of rat serumalbumin. In vivo studies on the formation of the disulfide bonds. J. Biol. Chem. 257, 8847-8853.
39. Rehaber, V., and Jaenicke, R. (1992). Stability and reconstitution of GAPDH from Thermotoga maritima. J. Biol. Chem. 267, 10999-11006.
40. Richards, F.M. (1992). Folded and unfolded proteins. In: Protein Folding, T.E. Creighton, ed. (New York: Freeman), pp. 1-58.
41. Roder, H., and Colón, W. (1997). Kinetic role of early intermediates in protein folding. Curr. Opin. Struct. Biol. 7, 15-28.
42. Rudolph, R., Nesslauer, G., Siebendritt, R., Sharma, A.K., Jaenicke, R. (1990). Folding of an all-β protein: Independent domain folding in γll-crystallin from calf eye lens. Proc. Natl. Acad. Sci. USA. 87, 4625-4629.
43. Rudolph, R., Böhm, G., Lilie, H., and Jaenicke, R. (1997). Folding proteins. In: Protein Function: A Practical Approach, T.E. Creighton, ed. (Oxford, UK.: IRL Press), pp. 57-99.
44. Schindler, T., Herrler, M., Marahiel, M.A., and Schmid, F.X. (1995). Extremely rapid folding in the absence of intermediates: The cold-shock protein from Bacillus subtilis. Nature Struct. Biol. 2, 663-673.
45. Seckler, R. (1997). Assembly of oligomers and multisubunit structures. In: Molecular Chaperones in the Life Cycle of Proteins. Fink, A.L. and Goto, Y., eds. (New York: M. Dekker) pp. 391-413.
46. Teschner, W., Rudolph, R. and Garel, J.-R. (1987). Intermediates on the folding pathway of ODH from Pecten jacobaeus. Biochemistry 26, 2791-2796.
47. Timasheff, S.N., and Arakawa, T. (1997). Stabilization of protein structure by solvents. In: Protein Function: A Practical Approach. T.E. Creighton, ed. (Oxford: IRL Press), pp. 349-364.
48. Wetlaufer, D.B. (1981). Folding of protein fragments. Adv. Protein Chem. 34, 61-92.
49. Wilson, G., Hecht, L., and Barron, L.D. (1996). Residual structure in unfolded proteins revealed by Raman optical activity. Biochemistry 35, 12518-12525.
50. Xue, Q., and Yeung, E.S. (1995). Differences in the chemical reactivity of individual molecules of an enzyme. Nature 373, 681-683.
51. Zettlmeissl, G., Rudolph, R., and Jaenicke, R. (1979). Reconstitution of LDH: Non-covalent aggregation vs reactivation. Biochemistry 18, 5567-5571.