Cold rescue of the thermolabile tailspike intermediate at the junction between productive folding and off-pathway aggregation

Protein Science

Volumn 7, Issue 7, 1998, Pages 1516-1523

  Betts, Scott D ^a   King, Jonathan ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

Bacteriophage P22; Endorhamnosidase; Inclusion body; Non native; Polymerization; Protein aggregation; Protein folding

Indexed keywords

ARTICLE; BACTERIOPHAGE; DISULFIDE BOND; ENZYME ACTIVITY; GEL ELECTROPHORESIS; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING;

EID: 0031854135     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070704     Document Type: Article

References (40)

1. Abola EE, Bernstein FC, Bryant SH, Koetzle TF, Weng J. 1987. Protein Data Bank. In: Allen FH, Bergerhoff G, Sievers R, eds. Crystallographic databases - Information content, software systems, scientific applications. Bonn: Data Commission of the International Union of Crystallography.
2. Beißinger M, Lee SC, Steinbacher S, Reinemer P, Huber R, Yu MH, Seckler R. 1995. Mutations that stabilize folding intermediates of phage P22 tailspike protein: Folding in vivo and in vitro, stability, and structural context. J Mol Biol 249:185-194.
3. Bennett MJ, Schlunegger MP, Eisenberg D. 1995. 3D domain swapping: A mechanism for oligomer assembly. Protein Sci 4:2455-2468.
4. Bernstein FC, Koetzle TF, Williams GJB, Meyer Jr EF, Brice MD, Rodgers JR, Kennard O, Shimanouchi T, Tasumi M. 1977. The protein data bank: A computer-based archival file for macromolecular structures. J Mol Biol 112:535-542.
5. Belts SD, Haase-Pettingell C, King JA. 1997. Mutational effects on inclusion body formation. Adv Protein Chem 50:243-264.
6. Blake C, Serpell L. 1996. Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous beta-sheet helix. Structure 4:989-998.
7. Brazil BT, Cleland JL, McDowell RS, Skelton, NJ, Paris K, Horowitz PM. 1997. Model peptide studies demonstrate that amphipathic secondary structures can be recognized by the chaperonin GroEL (cpn60). J Biol Chem 272:5105-5111.
8. Brems DN. 1988. Solubility of different folding conformers of bovine growth hormone. Biochemistry 27:4541-1546.
9. Brunschier R, Danner M, Seckler R. 1993. Interactions of phage P22 tailspike protein with GroE molecular chaperones during refolding in vitro. J Biol Chem 268:2767-2772.
10. Carrell RW, Lomas DA. 1997. Conformational disease. Lancet 350:134-138.
11. Danner M, Seckler R. 1993. Mechanism of phage P22 tailspike protein folding mutations. Protein Sci 2:1869-1881.
12. Ellis RJ, Hartl FU. 1996. Protein folding in the cell: Competing models of chaperonin function. FASEB J 10:20-26.
13. Fenton WA, Horwich AL. 1997. GroEL-mediated protein folding. Protein Sci 6:743-760.
14. Friguet B, Djavadi-Ohaniance L, Haase-Pettingell CA, King J, Goldberg ME. 1990. Properties of monoclonal antibodies selected for probing the conformation of wild type and mutant forms of the P22 tailspike endorhamnosidase. J Biol Chem 265:10347-10351.
15. Fuchs A, Seiderer C, Seckler R. 1991. In vitro folding pathway of phage P22 tailspike protein. Biochemistry 30:6598-6604.
16. Goldenberg D, King J. 1982. Trimeric intermediate in the in-vivo folding and subunit assembly pathways of the tailspike endorhamnosidase of bacteriophage P22. Proc Natl Acad Sci USA 79:3403-3407.
17. Goldenberg DP, Smith DH, King J. 1983. Genetic analysis of the folding pathway for the tailspike protein of phage P22. Prac Natl Acad Sci USA 80:7060-7064.
18. Haase-Pettingell CA, King J. 1988. Formation of aggregates from a thermolabile in vivo folding intermediate in P22 tailspike maturation a model for inclusion formation. J Biol Chem 263:4977-4983.
19. Haase-Pettingell C, King J. 1997. Prevalence of temperature sensitive folding mutations in the parallel β-coil domain of phage P22 tailspike endorhamnosidase. J Mol Biol 267:88-102.
20. Kelly JW. 1996. Alternative conformations of amyloidogenic proteins govern their behavior. Curr Opin Struct Biol 6:11-17.
21. King J, Haase-Pettingell C, Robinson AS, Speed M, Mitraki A. 1996. Thermolabile folding intermediates: Inclusion body precursors and chaperonin substrates. FASEB J 10:57-66.
22. King J, Yu M-H. 1986. Mutational analysis of protein folding pathways: The P22 tailspike endorhamnosidase. Methods Enzymol 131:250-266.
23. Lomas DA, Evans DL, Finch JT, Carrell RW. 1992. The mechanism of Z alpha 1-antitrypsin accumulation in the liver. Nature 357:605-607.
24. Marston FAO. 1986. The purification of eukaryotic polypeptides synthesized in Escherichia coli. Biochem J 240:1-12.
25. Mendoza JA, Lorimer GH, Horowitz PM. 1992. Chaperonin cpn60 from Escherichia coli protects the mitochondrial enzyme rhodanese against heat inactivation and supports folding at elevated temperatures. J Biol Chem 267:17631-17634.
26. Mitraki A, Betton JM, Desmadril M, Yon JM. 1987. Quasi-irreversibility in the unfolding-refolding transition of phosphoglycerate kinase induced by guanidine hydrochloride. Eur J Biochem 163:29-34.
27. Mitraki A, Fane B, Haase-Pettingell C, Sturtevant J, King J. 1991a. Global suppression of protein folding defects and inclusion formation. Science 253:54-58.
28. Mitraki A, Haase-Pettingell C, King J. 1991b. Mechanisms of inclusion body formation. In: Georgiou G, De Bernardez-Clark E, eds. Protein refolding. Washington: American Chemical Society, pp 35-49.
29. Mitraki A, King J. 1989. Protein folding intermediates and inclusion body formation. Biotechnology 7:690-697.
30. Oberg K, Chrunyk BA, Wetzel R, Fink AL. 1994. Nativelike secondary structure in interleukin-1β inclusion bodies by attenuated total reflectance FTIR. Biochemistry 33:2628-2634.
31. Robinson AS, King JA. 1997. Disulfide-bonded intermediate on the folding and assembly pathway of a non-disulfide bonded protein. Nat Struct Biol 4:450-455.
32. Sather SK, King J. 1994. Intracellular trapping of a cytoplasmic folding intermediate of the phage P22 tailspike using iodoacetamide. J Biol Chem 269:25268-25276.
33. Sauer RT, Krovatin W, Poteete AR, Berget PB. 1982. Phage P22 tail protein: Gene and amino acid sequence. Biochemistry 21:5811-5815.
34. Speed MA, Morshead T, Wang DI, King J. 1997. Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies. Protein Sci 6:99-108.
35. Speed MA, Wang DI, King J. 1995. Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chains. Protein Sci 4:900-908.
36. Speed MA, Wang DIC, King J. 1996. Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition. Nat Biotechnol 14:1283-1287.
37. Steinbacher S, Baxa U, Miller S, Weintraub A, Seckler R, Huber R. 1996. Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors. Proc Natl Acad Sci USA 93:10584-10588.
38. Steinbacher S, Seckler R, Miller S, Steipe B, Huber R, Reinemer P. 1994. Crystal structure of P22 tailspike protein: Interdigitated subunits in a thermostable trimer. Science 265:383-386.
39. Wetzel R. 1994. Mutations and off-pathway aggregation of proteins. Trends Biotechnol 12:193-198.
40. Xie Y, Wetlaufer DB. 1996. Control of aggregation in protein refolding: The temperature-leap tactic. Protein Sci 5:517-523.