Structural studies of MS2 bacteriophage virus particle disassembly by nuclear magnetic resonance relaxation measurements

Biophysical Journal

Volumn 84, Issue 6, 2003, Pages 3894-3903

  Anobom, C D ^c   Albuquerque, S C ^c   Albernaz, F P ^c   Oliveira, A C ^c   Silva, J L ^c   Peabody, D S ^a   Valente, A P ^b   Almeida, F C L ^b  

^a UNIVERSITY OF NEW MEXICO SCHOOL OF MEDICINE   (United States)

^b FEDERAL UNIVERSITY OF RIO DE JANEIRO   (Brazil)

^c NONE

Author keywords

[No Author keywords available]

Indexed keywords

COAT PROTEIN; DIMER;

ARTICLE; CIRCULAR DICHROISM; CONFORMATION; DISSOCIATION; ESCHERICHIA COLI; FLUORESCENCE; MEASUREMENT; MS2 VIRUS; NONHUMAN; PH; PROTON NUCLEAR MAGNETIC RESONANCE; STEADY STATE; TEMPERATURE; VIRUS ASSEMBLY; VIRUS MORPHOLOGY; VIRUS PARTICLE;

ESCHERICHIA COLI; RNA VIRUSES; UNIDENTIFIED BACTERIOPHAGE;

EID: 0037763947     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)75117-0     Document Type: Article

References (31)

1. Akke, M., and A. G. Palmer. 1996. Monitoring macromolecular motions on microsecond to millisecond time scales by R(1), Rho R(1) constant relaxation time NMR spectroscopy J. Am. Chem. Soc. 118:911-912.
2. 15N labeled protein with heteronuclear two-dimensional spectroscopy. J. Magn. Res. 124:509-511.
3. Almeida, F. C., and S. J. Opella. 1997b. FD coat protein structure in membrane environments: structural dynamics of the loop between the hydrophobic trans membrane helix and the amphipathic in-plane helix. J. Mol. Biol. 270:481-495.
4. Atkins, P. W., editor. 1997. Physical Chemistry, 6th Ed. W. H. Freeman & Co., London.
5. Axblom, C., K. Tars, K. Fridborg, L. Oma, M. Bundule, and L. Liljas. 1998. Structure of phage FR capsids with deletion in the FG loop: implications for viral assembly. Virology. 249:80-88.
6. Berglund, H., H. Kovács, K. Dahlman-Wright, J. Gustafsson, and T. Hãrd. 1992. Backbone dynamics of the glucocorticoid receptor DNA-binding domain. Biochemistry. 31:12001-12011.
7. 1H NMR spectroscopy. Biochemistry. 29:7387-7401.
8. Clore, G. M., A. Szabo, A. Bax, L. E. Kay, P. C. Driscoll, and A. M. Gronenborn. 1990b. Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins. J. Am. Chem. Soc. 112:4989-4991.
9. DaPoian, A. T., A. C. Oliveira, P. L. Gaspar, J. L. Silva, and G. Weber. 1993. Reversible pressure dissociation of R17 bacteriophage: the physical individuality of virus particles. J. Mol. Biol. 31:999-1008.
10. Golmohammadi, R., K. Valegard, K. Fridborg, and L. Liljas. 1993. The refined structure of bacteriophage MS2 at 2.8 Å resolution. J. Mol. Biol. 234:620-639.
11. Johnson, J. E., and W. Chiu. 2000. Structures of virus and virus-like particles. Curr. Opin. Struct. Biol. 10:229-235.
12. Johnson, W. C., Jr. 1988. Secondary structure of proteins through circular dichroism. Ann. Rev. Biophys. Chem. 17:145-167.
13. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature. 277:680-700.
14. Lago, H., A. M. Parrott, T. Moss, N. J. Stonehouse, and P. G. Stockley. 2001. Probing the kinetics of formation of the bacteriophage MS2 translational operator complex: identification of a protein conformer unable to bind RNA. J. Mol. Biol. 305:1131-1144.
15. Liljas, L. 1999. Virus assembly. Curr. Opin. Struct. Biol. 9:129-134.
16. Lipari, G., and A. Szabo. 1982. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104:4546-4559.
17. Lowry, O. H., N. J. Rosenbrough, A. L. Farr, and R. J. Randall. 1951. Protein measurement with the folin phenol reagent. J. Biol. Chem. 193: 265-275.
18. Mandel, A. M., M. Akke, and A. G. Palmer. 1996. Dynamics of ribonuclease H: temperature dependence of motions on multiple time scales. Biochemistry. 35:16009-16023.
19. Ni, C. Z., R. Syed, R. Rondandapanir, J. Wickersham, D. S. Peabody, and K. R. Ely. 1995. Crystal-structure of the MS2 coat protein dimer implications for RNA binding and virus assembly. Structure. 3:255-263.
20. Nirmala, N. R., and G. Wagner. 1998. Measurement of C-13 relaxation times in proteins by two-dimensional heteronuclear H1-C13 correlation spectroscopy. J. Am. Chem. Soc. 110:7557-7558.
21. Peabody, D. S., and K. R. Ely. 1992. Control of translational repression by protein-protein interactions. Nucleic Acids Res. 20:1649-1655.
22. Phelps, K., B. Speelman, and C. B. Post. 2000. Theoretical studies of viral capsid proteins. Curr. Opin. Struct. Biol. 10:170-173.
23. Privalov, P. L. 1996. Intermediate states in protein folding. J. Mol. Biol. 258:707-725.
24. 15N NMR relaxation measurement. Biochemistry. 31:4394-4406.
25. Stonehouse, N. J., K. Valegard, R. Golmohammadi, S. van den Worm, C. Walton, P. G. Stockey, and L. Liljas. 1996. Crystal structures of MS2 capsids with mutations in the subunit FG loop. J. Mol. Biol. 256:330-339.
26. Sugiyama, T., R. R. Hebert, and K. A. Hartman. 1967. Ribonucleoprotein complexes formed between bacteriophages MS2 RNA and MS2 coat protein in vitro. J. Mol. Biol. 25:455-463.
27. Tuma, R., J. H. K. Bamford, D. H. Bamford, M. P. Russel, and G. J. Thomas, Jr. 1996. Structure interaction and dynamics of PRD1 virus. I. Coupling of subunit folding and capsid assembly. J. Mol. Biol. 257:87-101.
28. van Vlijmen, H. W. T., S. Curry, M. Schaefer, and M. Karpuls. 1998. Titration calculations of foot-and-mouth disease virus capsid and their stabilities as a function of pH. J. Mol. Biol. 275:295-308.
29. Valegard, K., L. Liljas, K. Fridborg, and T. Unge. 1990. The three-dimensional structure of the icosahedral bacterial virus MS2. Nature. 345:36-41.
30. Wagner, G. 1993. Characterization of the distribution of internal motions in the basic pancreatic trypsin inhibitor using a large number of internal NMR probes. Quar. Rev. Biophys. 16:1-57.
31. Wagner, G., S. Hyberts, and J. W. Peng. 1993. Study of protein dynamics by NMR. In NMR of Proteins. G. M. Clore, and A. M. Gronenborn, editors. CRC Press, Boca Raton, FL. p. 220.