Nonnative Interactions between Cysteines Direct Productive Assembly of P22 Tailspike Protein

Biophysical Journal

Volumn 85, Issue 5, 2003, Pages 3237-3247

  Danek, Brenda L ^a   Robinson, Anne Skaja ^a  

^a University of Delaware   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE; PROTEIN P22 TAILSPIKE; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN INTERACTION;

BACTERIA (MICROORGANISMS); NEGIBACTERIA;

EID: 0242290827     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74741-9     Document Type: Article

References (26)

1. Benton, C. B., J. A. King, and P. L. Clark. 2002. Characterization of the protrimer intermediate in the folding pathway of the interdigitated beta-helix tailspike protein. Biochemistry. 41:5093-5103.
2. Betts, S., and J. A. King. 1998. Cold rescue of the thermolabile tailspike intermediate at the junction between productive folding and off-pathway aggregation. Protein Sci. 7:1516-1523.
3. Danner, M., and R. Seckler. 1993. Mechanism of phage P22 tailspike protein folding mutations. Protein Sci. 2:1869-1881.
4. Fane, B., R. Villafane, et al. 1991. Identification of global suppressors for temperature-sensitive folding mutations of the P22 tailspike protein. J. Biol. Chem. 266:11640-11648.
5. Gage, M., and A. S. Robinson. 2003. C-terminal hydrophobic interactions play a critical role in oligomeric assembly of the P22 tailspike trimmer. Protein Sci. In press.
6. Gilbert, H. F. 1990. Molecular and cellular aspects of thiol-disulfide exchange. Adv. Enzymol. Relat. Areas Mol. Biol. 63:69-172.
7. Goldenberg, D., P. B. Berget, and J. King. 1982. Maturation of the tail spike endorhamnosidase of Salmonella phage P22. J. Biol. Chem. 257:7864-7871.
8. Goldenberg, D., and J. A. King. 1982. 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.
9. Goldenberg, D., D. H. Smith, et al. 1983. Genetic analysis of the folding pathway for the tail spike phage P22. Proc. Natl. Acad. Sci. USA. 80:7060-7064.
10. Haase-Pettingell, C., S. Betts, et al. 2001. Role for cysteine residues in the in vivo folding and assembly of the phage P22 tailspike. Protein Sci. 10:397-410.
11. King, J. A., and M.-H. Yu. 1986. Mutational analysis of protein folding pathway using the P22 tailspike endorhamnosidase. Methods Enzymol. 131:250-266.
12. Lefebvre, B. G., and A. S. Robinson. 2003. Pressure treatment of tailspike aggregates rapidly produces on-pathway folding intermediates. Biotechnol. Bioeng. 82:595-604.
13. Li, P. P., A. Nakanishi, et al. 2002. Formation of transitory intrachain and interchain disulfide bonds accompanies the folding and oligomerization of simian virus 40 Vp1 in the cytoplasm. Proc. Natl. Acad. Sci. USA. 99:1353-1358.
14. Mitraki, A., M. Danner, et al. 1993. Temperature-sensitive mutations and second-site suppressor substitutions affect folding of the P22 tailspike protein in vitro. J. Biol. Chem. 268:20071-20075.
15. Mitraki, A., B. Fane, et al. 1991. Global suppression of protein folding defects and inclusion body formation. Science. 253:54-58.
16. Raso, S. W., P. L. Clark, C. Haase-Pettingell, J. King, G. J. Thomas, Jr. 2001. Distinct cysteine sulfhydryl environments detected by analysis of Raman S-H markers of Cys->Ser mutant proteins. J. Mol. Biol. 307:899-911.
17. Robinson, A. S., and J. A. King. 1997. Disulphide-bonded intermediate on the folding and assembly pathway of a non-disulphide bonded protein. Nat. Struct. Biol. 4:450-455.
18. Sambrook, J., E. F. Fritsch, et al. 1989. Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
19. Sargent, D., J. M. Benevides, M. H. Yu, J. King, G. J. Thomas, Jr. 1988. Secondary structure and thermostability of the phage P22 tailspike. XX. Analysis of Raman spectroscopy of the wild-type protein and a temperature-sensitive folding mutant. J. Mol. Biol. 199:491-502.
20. Sather, S., and J. A. King. 1994. Intracellular trapping of a cytoplasmic folding intermediate of the phage P22 tailspike using iodoacetamide. J. Biol. Chem. 269:25268-25276.
21. Seckler, R., A. Fuchs, et al. 1989. Reconstitution of the thermostable trimeric phage P22 tailspike protein from denatured chains in vitro. J. Biol. Chem. 264:11750-11753.
22. Speed, M. A., T. Morshead, et al. 1997. Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies. Protein Sci. 6:99-108.
23. Speed, M. A., D. I. C. Wang, et al. 1995. Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chains. Protein Sci. 4:900-908.
24. Steinbacher, S., R. Seckler, et al. 1994. Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer. Science. 265:383-386.
25. Weaver, J. C. 1993. Electroporation: a general phenomenon for manipulating cells and tissues. J. Cell. Biochem. 51:426-435.
26. Xie, Y., and D. B. Wetlaufer. 1996. Control of aggregation in protein refolding: the temperature-leap tactic. Protein Sci. 5:517-523.