Disulphide-bonded intermediate on the folding and assembly pathway of a non-disulphide bonded protein

Nature Structural Biology

Volumn 4, Issue 6, 1997, Pages 450-455

  Robinson, Anne Skaja ^a   King, Jonathan ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; DISULFIDE BOND; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FOLDING; PROTEIN QUATERNARY STRUCTURE;

CYSTEINE; DIMERIZATION; DISULFIDES; EDETIC ACID; EGTAZIC ACID; ELECTROPHORESIS; GLYCOSIDE HYDROLASES; METALS; MODELS, MOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; SULFHYDRYL COMPOUNDS; SULFUR RADIOISOTOPES; VIRAL TAIL PROTEINS;

EID: 0030900095     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0697-450     Document Type: Article

References (35)

1. Creighton, T.E. Proteins. Structures and Molecular Properties. 2nd ed. (W.H. Freeman and Company, New York, 1993).
2. Braakman, I., Hoover-Litty, H., Wagner, K.R., & Helenius, A. Folding of influenza hemagglutinin in the endoplasmic reticulum. J. Cell Biol. 114, 401-411 (1991).
3. Creighton, T.E. Conformation restrictions on the pathway of folding and unfolding of the pancreatic trypsin inhibitor. J. Mol. Biol., 113, 275-293 (1977).
4. Creighton, T.E. Effects of urea and guanidine-HCl on the folding and unfolding of pancreatic trypsin inhibitor. J. Mol. Biol. 113, 313-328 (1977).
5. Creighton, T.E. &Goldenberg, D.P. Kinetic role of a meta-stable native-like two-disulphide species in the folding transition of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 179, 497-526 (1984).
6. Weissman, J.S. & Kim, P.S. The pro region of BPTI facilitates folding. Cell 71, 841-851 (1992).
7. Weissman, J.S. &Kim, P.S. Reexamination of the folding of BPTI: Predominance of native intermediates. Science 253, 1386-1393 (1991).
8. Fahey, R.C., Hunt, J.S., & Windham, G.C. On the cysteine and cystine content of proteins: Differences between intracellular and extracellular proteins. J. Mol. Evol. 10, 155-160 (1977).
9. Gilbert, H.F. Molecular and cellular aspects of thiol-disulfide exchange. in Advances in Enzymology (ed. Meister, A.) 69-173 (Wiley, New York, 1990).
10. Grubmeyer, C.T. & Gray, W.R. A cysteine residue (cysteine-116) in the histidinol binding site of histidinol dehydrogenase. Biochemistry 25, 4778-4784 (1986).
11. Sauer, R.T., Krovatin, W., Poteete, A.R., & Berget, P.B. Phage P22 tail protein: Gene and amino acid sequence. Biochemistry 21, 5811-5815 (1982).
12. Steinbacher, S. et al. Crystal structure of P22 tailspike protein: Interdigitated subunits in a thermostable trimer. Science 265, 383-386 (1994).
13. Yoder, M.D., Keen, N.T., & Jurnak, R. New domain motif: The structure of pectate lyase C, a secreted plant virulence factor. Science 260, 1503-1507 (1993).
14. Baumann, U., Wu, S., Flaherty, K.M., & McKay, D.B. Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif. EMBO J. 12, 3357-3364 (1993).
15. Goldenberg, D., Berget, P., & King, J. Maturation of the tailspike endrorhamnoside of Salmonella phage P22. J. Biol. Chem. 257, 7864-7871 (1982).
16. Goldenberg, D. & King, J. Trimeric intermediate in the in vivo folding and subunit assembly of the tail spike endorhamnosidase of bacteriophage P22. Proc. Natl. Acad. Sci. USA 79, 3403-3407 (1982).
17. Haase-Pettingell, C.A. & King, J. Formation of aggregates from a thermolabile in-vivo folding intermediate in P22 tailspike maturation a model for inclusion body formation. J. Biol. Chem. 263, 4977-4983 (1988).
18. Seckler, R., Fuchs, A., King, J. & Jaenicke, R. Reconstitution of the thermostable trimeric phage P22 tailspike protein from denatured chains in vitro. J. Biol. Chem. 264, 11750-11753 (1989).
19. Fuchs, A., Seiderer, C. & Seckler, R. In vitro folding pathway of phage P22 tailspike protein. Biochemistry 30, 6598-6604 (1991).
20. Speed, M.A., Wang, D.I.C. & King, J. Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chains. Prot. Sci. 4, 900-908 (1995).
21. Danner, M. & Seckler, R. Mechanism of phage P22 tailspike protein folding mutations. Prot. Sci. 2, 1869-1881 (1993).
22. Goldenberg, D.P., Smith, D.H. & King, J. Genetic analysis of the folding pathway for the tail spike of phage P22. Proc. Natl. Acad. Sci. USA 80, 7060-7064 (1983).
23. Sargent, D., Benevides, J.M., Yu, M.-H., King, J. & Thomas Jr., G.J.T. Secondary structure and thermostability of the phage P22 tailspike: Analysis of raman spectroscopy of the wild type protein and a temperature-sensitive folding mutant. J. Mol. Biol. 199, 491-502 (1988).
24. Sather, S.K. & King, J. Intracellular trapping of a cytoplasmic folding intermediate of the phage P22 tailspike using iodoacetamide. J. Biol. Chem. 269, 25268-25276 (1994).
25. Lippard, S.J. & Berg, J.M. Principles of Bioinorganic Chemistry. (University Science Books, Mill Valley, California, 1994).
26. Hwang, C., Sinskey, A.J. & Lodish, H.F. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257, 1496-1502 (1992).
27. Gilbert, H.F. The formation of native disulfide bonds. in Mechanisms of Protein Folding (ed. Pain, R.H.) 104-136 (IRL Press, New York, 1994).
28. Derman, A.I., Prinz, W.A., Belin, D. & Beckwith, J. Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science 262, 1744-1747 (1993).
29. Freedman, R.B. Protein folding in the cell in Protein Folding (ed. Creighton, T.E.) 455-539 (W.H. Freeman and Company, New York, 1992).
30. Winston, R., Botstein, D. & Miller, J. Characterization of amber and ochre suppressors in Salmonella typhimurium. J. Bacteriol. 137, 433-439 (1979).
31. King, J. &Yu, M.-H. Mutational analysis of protein folding pathway using the P22 tailspike endorhamnosidase in Methods in Enzymology (eds Hirs, C.W.H. & Timashiff, S.) 250-266 (Academic Press, New York, 1986).
32. Yamamoto, K.R., Alberts, B.M., Benzinger, B., Lawhorne, L., & Treiber, G. Rapid bacteriophage sedimentation in the presence of polyethylene glycol and its application to large-scale virus purification. Virology 40, 734-744 (1970).
33. Sambrook, J., Fritsch, E.F. & Maniatis, T. Molecular Cloning, A Laboratory Manual. (Cold Spring Harbor Laboratory Press, New York, 1989).
34. Kirley, T.L. Reduction and fluorescent labeling of cysteine-containing proteins for subsequent structural analyses. Anal. Biochem. 180, 231-236 (1989).
35. Koradi, R., Billeter, M., & Wüthrich, K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55 (1996).