1887

Abstract

Vibrational Raman optical activity (ROA) spectra of tobacco rattle virus (TRV) and tobacco mosaic virus (TMV) were measured and compared with a view to obtaining new information about the coat protein subunit structure of TRV. A sharp strong positive band observed at ∼1344 cm in the ROA spectra of the two viruses is evidence that both contain a significant amount of a hydrated form of α-helix, but more in TRV than in TMV. Although the ROA spectrum of TMV shows significant positive intensity in the range ∼1297–1312 cm characteristic of α-helix in a hydrophobic environment, as expected from the helix interface residues in the four-helix bundles that constitute the basic motif of the TMV coat protein fold, that of TRV shows little positive ROA intensity here. Instead TRV shows a strong positive ROA band at ∼1315 cm, of much greater intensity than bands shown here by TMV, that is characteristic of polyproline II (PPII) helix. This suggests that the additional long central and C-terminal sequences of the TRV coat proteins contain a significant amount of PPII structure, plus perhaps some β-strand judging by a prominent sharp negative ROA band shown by TRV at ∼1236 cm, but little α-helix. The open flexible hydrated nature of PPII helical structure is consistent with the earlier suggestions that the additional sequences are exposed and, together with a larger amount of hydrated α-helix, could serve to fill the extra volume required by the larger diameter of the cylindrical TRV particles relative to those of TMV.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-82-6-1499
2001-06-01
2021-10-24
Loading full text...

Full text loading...

/deliver/fulltext/jgv/82/6/0821499a.html?itemId=/content/journal/jgv/10.1099/0022-1317-82-6-1499&mimeType=html&fmt=ahah

References

  1. Adzhubei A. A., Sternberg M. J. E. 1993; Left-handed polyproline II helices commonly occur in globular proteins. Journal of Molecular Biology 229:472–493
    [Google Scholar]
  2. Barron L. D., Hecht L., Blanch E. W., Bell A. F. 2000; Solution structure and dynamics of biomolecules from Raman optical activity. Progress in Biophysics & Molecular Biology 73:1–49
    [Google Scholar]
  3. Bergethon P. R. 1998 The Physical Basis of Biochemistry New York: Springer-Verlag;
  4. Blanch E. W., Bell A. F., Hecht L., Day L. A., Barron L. D. 1999; Raman optical activity of filamentous bacteriophages: hydration of α-helices. Journal of Molecular Biology 290:1–7
    [Google Scholar]
  5. Blanch E. W., Morozova-Roche L. A., Hecht L., Noppe W., Barron L. D. 2000a; Raman optical activity characterization of native and molten globule states of equine lysozyme: comparison with hen lysozyme and bovine α-lactalbumin. Biopolymers (Biospectroscopy 57:235–248
    [Google Scholar]
  6. Blanch E. W., Morozova-Roche L. A., Cochran D. A. E., Doig A. J., Hecht L., Barron L. D. 2000b; Is polyproline II helix the killer conformation? A Raman optical activity study of the amyloidogenic prefibrillar intermediate of human lysozyme. Journal of Molecular Biology 301:553–563
    [Google Scholar]
  7. Boedker H., Simmons N. S. 1958; Preparation and characterization of essentially uniform tobacco mosaic virus particles. Journal of the American Chemical Society 80:2550–2556
    [Google Scholar]
  8. Goulden M. G., Davies J. W., Wood K. R., Lomonossoff G. P. 1992; Structure of tobraviral particles: a model suggested from sequence conservation in tobraviral and tobamoviral coat proteins. Journal of Molecular Biology 227:1–8
    [Google Scholar]
  9. Hecht L., Barron L. D., Blanch E. W., Bell A. F., Day L. A. 1999; Raman optical activity instrument for studies of biopolymer structure and dynamics. Journal of Raman Spectroscopy 30:815–825
    [Google Scholar]
  10. Klug A. 1999; The tobacco mosaic virus particle: structure and assembly. Philosophical Transactions of the Royal Society of London B Biological Sciences 354:531–535
    [Google Scholar]
  11. Legorburu F. J., Robinson D. J., Torrance L. 1996; Features on the surface of the tobacco rattle tobravirus particle that are antigenic and sensitive to proteolytic digestion. Journal of General Virology 77:855–859
    [Google Scholar]
  12. Mayo M. A., Brierley K. M., Goodman B. A. 1993; Developments in the understanding of the particle structure of tobraviruses. Biochimie 75:639–644
    [Google Scholar]
  13. Morozova-Roche L. A., Arico-Muendel C. C., Haynie D. T., Emelyanenko V. I., Van Dael H., Dobson C. M. 1997; Structural characterization and comparison of the native and A-states of equine lysozyme. Journal of Molecular Biology 268:903–921
    [Google Scholar]
  14. Roberts I. M., Mayo M. A. 1980; Electron microscope studies of the structure of the disk aggregate of tobacco rattle virus protein. Journal of Ultrastructure Research 71:49–59
    [Google Scholar]
  15. Robinson D. J. 1983; RNA species of tobacco rattle virus strains and their nucleotide sequence relationships. Journal of General Virology 64:657–665
    [Google Scholar]
  16. Smyth E., Syme C. D., Blanch E. W., Hecht L., Vãsák M., Barron L. D. 2001; Solution structure of native proteins with irregular folds from Raman optical activity. Biopolymers 58:138–151
    [Google Scholar]
  17. Stapley B. J., Creamer T. P. 1999; A survey of left-handed polyproline II helices. Protein Science 8:587–595
    [Google Scholar]
  18. Stubbs G. 1999; Tobacco mosaic virus particle structure and the initiation of disassembly. Philosophical Transactions of the Royal Society of London B Biological Sciences 354:551–557
    [Google Scholar]
  19. Thomas G.J. Jr 1999; Raman spectroscopy of protein and nucleic acid assemblies. Annual Review of Biophysics and Biomolecular Structure 28:1–27
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-82-6-1499
Loading
/content/journal/jgv/10.1099/0022-1317-82-6-1499
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error