Partially folded states of the capsid protein of cowpea severe mosaic virus in the disassembly pathway

Journal of Molecular Biology

Volumn 273, Issue 2, 1997, Pages 456-466

  Gaspar, Luciane P ^a   Johnson, John E ^b   Silva, Jerson L ^a   Da Poian, Andrea T ^a  

^a FEDERAL UNIVERSITY OF RIO DE JANEIRO   (Brazil)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Cold denaturation; Fluorescence; Pressure; Protein RNA interaction; Virus assembly

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; CAPSID PROTEIN; COAT PROTEIN; RIBONUCLEASE; TRYPSIN; UREA; VIRUS RNA;

ARTICLE; CONTROLLED STUDY; FLUORESCENCE; HYDROSTATIC PRESSURE; MOSAIC VIRUS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN RNA BINDING; TEMPERATURE; VIRUS ASSEMBLY;

COWPEA SEVERE MOSAIC VIRUS; MIRIDAE;

EID: 0030785560     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1299     Document Type: Article

References (47)

1. Beechen J. M., Gratton E., Ameloot M., Knutson J. R., Brand L. The global analysis of fluorescence intensity and anisotropy decay data: second-generation theory and programs. Topics in Fluorescence Spectroscopy. Volume 2: Principles. 1991;Plenum Press, New York.
2. Bonafe C. F. S., Villas-Boas M. S., Suarez M. C., Silva J. L. Reassembly of a large multisubunit protein promoted by nonprotein factors. Effects of calcium and glycerol on the association of extracellular hemoglobin. J. Biol. Chem. 266:1991;13210-13216.
3. Bonafe C. F. S., Araujo J. R. V., Silva J. L. Intermediates states of assembly in the dissociation of gastropod hemocyanin by hydrostatic pressure. Biochemistry. 33:1994;2651-2660.
4. Braig K., Otwinowski Z., Hegde R., Boisvert D. C., Joachimiak A., Horwich X. X., Sigler P. B. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å Nature. 371:1994;578-586.
5. Chen X., Bruening G. Nucleotide sequence and genetic map of cowpea severe mosaic virus RNA2 and comparisons with RNA2 of others comoviruses. Virology. 187:1992;682-692.
6. Chen Z., Stauffacher C. V., Li Y., Schimidt T., Bomu W., Kamer G., Shanks M., Lomonossoff G., Johnson J. E. Protein-RNA interactions in an icosahedral virus at 3.0 Å resolution. Science. 245:1989;154-159.
7. Chen Z., Stauffacher C. V., Schmidt T., Fisher A., Johnson J. E. RNA packing in bean pod mottle virus. Brinton M. A., Heinz F. X. New Aspects of Positive-Strand RNA Viruses. 1990;American Society for Microbiology, Washington.
8. Clery C., Renault F., Masson P. Pressure-induced molten globule state of cholinesterase. FEBS Letters. 370:1995;212-214.
9. Cohen C. C., McCormick F. P. Polyamines and virus multiplication. Advan. Virus Res. 24:1979;331-387.
10. Da Poian A. T., Oliveira A. C., Gaspar L. P., Silva J. L., Weber G. Reversible pressure dissociation of R17 bacteriophage: The physical individuality of virus particles. J. Mol. Biol. 291:1993;999-1008.
11. Da Poian A. T., Johnson J. E., Silva J. L. Differences in pressure stability of the three components of cowpea mosaic virus: implications for virus assembly and disassembly. Biochemistry. 33:1994;8339-8346.
12. Da Poian A. T., Oliveira A. C., Silva J. L. Cold denaturation of an icosahedral virus. The role of entropy in virus assembly. Biochemistry. 34:1995;2672-2677.
13. de Jager C. P. Cowpea severe mosaic virus. Harrinson B. D., Murant A. F. Descriptions of Plant Viruses. 1979;no. 209, Commonwealth Mycological Institute and Association of Applied Biologists (CMI/AAB) Kew, UK.
14. Draper D. E. Protein-RNA recognition. Annu. Rev. Biochem. 64:1995;593-620.
15. Eggen R., van Kammen A. RNA replication in comoviruses. Ahlquist P., Holland J. J., Domingo E. RNA Genetics. 1988.
16. Foguel D., Silva J. L. Cold denaturation of Arc repressor operator complex: The role of entropy on protein DNA-recognition. Proc. Natl Acad. Sci. USA. 91:1994;8244-8247.
17. Foguel D., Weber G. Pressure-induced dissociation and denaturation of allophycocyanin at sub-zero temperatures. J. Biol. Chem. 270:1995;28759-28766.
18. Foguel D., Chaloub R. M., Silva J. L., Crofts A. R., Weber G. Pressure and low temperature effects on the fluorescence emission spectra and lifetimes of the photosynthetic components of cyanobacteria. Biophys. J. 63:1992;1613-1622.
19. Gratton E., Alcala J. R., Marriott G. Rotations of tryptophan residues in proteins. Biochem. Soc. Trans. 14:1986;835-838.
20. Gross M., Jaenicke R. Proteins under pressure. The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes. Eur. J. Biochem. 221:1994;617-630.
21. Fulton J. P., Scott H. A. A serogrouping concept for legume comoviruses. Phytopathology. 69:1979;305-306.
22. King L., Weber G. Conformational drift of dissociated lactate dehydrogenase. Biochemistry. 25:1986;3632-3637.
23. Lundbäck L., Härd T. Sequence-specific DNA binding dominated by dehydration. Proc. Natl Acad. Sci. USA. 93:1996;4754-4759.
24. Mozhaev V. V., Heremans K., Frank J., Masson P., Balny C. Exploiting the effects of hydrostatic pressure in biotechnological applications. Trends Biotechnol. 12:1994;493-501.
25. Nagai K. RNA-protein complexes. Curr. Opin. Struct. Biol. 6:1996;53-61.
26. Paladini A. A., Weber G. Pressure-induced reversible dissociation of enolase. Biochemistry. 20:1981;2587-2593.
27. 1. Proc. Natl Acad. Sci. USA. 90:1993;1776-1780.
28. Prevelige P., King J., Silva J. L. Pressure denaturation of bacteriophage P22 coat protein and its entropic stabilization in the icosahedral shells. Biophys. J. 66:1994;1631-1641.
29. Privalov P. L. Cold denaturation of proteins. Crit. Rev. Biochem. Mol. Biol. 25:1990;281-305.
30. Robinson C. R., Sligar S. G. Hydrostatic and osmotic pressure as tools to study macromolecular recognition. Methods in Enzymology, Energetics of Biological Macromolecules. 1995;Academic Press, New York.
31. Rosen C. G., Weber G. Dimer formation from 1-anilino-8-naphthalene sulfonate catalyzed by bovine serum albumin. A new fluorescent molecule with exceptional binding properties. Biochemistry. 8:1969;3915-3920.
32. Rossmann M. G., Abad-Zapatero C., Hermodson M. A., Erickson J. W. Subunit interactions in southern bean mosaic virus. J. Mol. Biol. 166:1983;37-83.
33. Ruan K., Weber G. Dissociation of yeast hexokinase by hydrostatic pressure. Biochemistry. 27:1988;3295-3301.
34. Schmidt T., Johnson J. E., Phillips W. E. The spherically averaged structures of cowpea mosaic virus components by X-ray solution scattering. Virology. 127:1983;65-73.
35. Siler D. J., Babcock J., Bruening G. Electrophoretic mobility and enhanced infectivity of a mutant of cowpea mosaic virus. Virology. 71:1976;560-567.
36. Silva J. L. The drift and molten-globule state of proteins dissociated by pressure. Braz. J. Med. Biol. Res. 26:1993;383-393.
37. Silva J. L., Silveira M. C. F. Energy coupling between DNA binding and subunit association is responsible for the specificity of DNA-Arc interactions. Protein Sci. 2:1993;945-950.
38. Silva J. L., Weber G. Pressure-induced dissociation of brome mosaic virus. J. Mol. Biol. 199:1988;149-161.
39. Silva J. L., Weber G. Pressure stability of proteins. Annu. Rev. Phys. Chem. 44:1993;89-113.
40. Silva J. L., Miles E. W., Weber G. Pressure dissociation and conformation drift of the β-dimer of tryptophan synthase. Biochemistry. 25:1986;5780-5786.
41. Silva J. L., Villas-Boas M., Bonafe C. F. S., Meireles N. C. Anomalous pressure dissociation of large protein aggregates. Lack of concentration dependence and irreversibility at extreme degrees of dissociation of extracellular hemoglobin. J. Biol. Chem. 264:1989;15863-15868.
42. Silva J. L., Silveira C. F., Correia A., Pontes L. Dissociation of a native dimer to a molten globule monomer. Effects of pressure and dilution on the association equilibrium of Arc repressor. J. Mol. Biol. 233:1992;545-555.
43. Silva J. L., Foguel D., Da Poian A. T., Prevelige P. E. The use of hydrostatic pressure as a tool to study viruses and other macromolecular assemblages. Curr. Opin. Struct. Biol. 6:1996;166-175.
44. Speir J. A., Munshi S., Wang G., Baker T. S., Johnson J. E. Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo-electron microscopy. Structure. 3:1995;63-78.
45. Weber G. Phenomenological description of the association of protein subunits subjected to conformational drift. Effects of dilution and hydrostatic pressure. Biochemistry. 25:1986;3626-3631.
46. White J. M., Johnson J. E. Crystalline cowpea mosaic virus. Virology. 101:1980;319-324.
47. Williams R. K., Shen C. The effect of pressure on the activity of ribonuclease. Arch. Biochem. Biophys. 152:1972;606-612.