Display options
Cite
Shire SJ, Stegkert JJ, Schuster TM. Mechanism of tobacco mosaic virus assembly: Incorporation of 4S and 20S protein at pH 7.0 and 20 degrees C. Proc Natl Acad Sci U S A. 1981;78(1):256-60doi: 10.1073/pnas.78.1.256.
Shire, S. J., Stegkert, J. J., & Schuster, T. M. (1981). Mechanism of tobacco mosaic virus assembly: Incorporation of 4S and 20S protein at pH 7.0 and 20 degrees C. Proceedings of the National Academy of Sciences of the United States of America, 78(1), 256-60. https://doi.org/10.1073/pnas.78.1.256
Shire, S J, et al. "Mechanism of tobacco mosaic virus assembly: Incorporation of 4S and 20S protein at pH 7.0 and 20 degrees C." Proceedings of the National Academy of Sciences of the United States of America vol. 78,1 (1981): 256-60. doi: https://doi.org/10.1073/pnas.78.1.256
Shire SJ, Stegkert JJ, Schuster TM. Mechanism of tobacco mosaic virus assembly: Incorporation of 4S and 20S protein at pH 7.0 and 20 degrees C. Proc Natl Acad Sci U S A. 1981 Jan;78(1):256-60. doi: 10.1073/pnas.78.1.256. PMID: 16592945; PMCID: PMC319031.
Copy Download .nbib Format: NLM
Share it on

Proc Natl Acad Sci U S A. 1981 Jan;78(1):256-60. doi: 10.1073/pnas.78.1.256.

Mechanism of tobacco mosaic virus assembly: Incorporation of 4S and 20S protein at pH 7.0 and 20 degrees C.

Proceedings of the National Academy of Sciences of the United States of America

S J Shire, J J Stegkert, T M Schuster

Affiliations

  1. Biochemistry and Biophysics Section, Biological Sciences Group, University of Connecticut, Storrs, Connecticut 06268.

PMID: 16592945 PMCID: PMC319031 DOI: 10.1073/pnas.78.1.256

Abstract

The mechanism of assembly of tobacco mosaic virus (TMV) has been investigated at pH 7.0 and 20 degrees C by analytical ultracentrifugation. Under these conditions the overall rates of interconversion of 4S and 20S TMV coat protein are sufficiently slow to make possible measurements of the concentrations of remaining 4S and 20S TMV coat protein after addition of homologous RNA to solutions containing, initially, various mass ratios of 20S protein to 4S protein. It has been possible to measure, by schlieren boundary analysis, the relative rates of incorporation of 4S and 20S TMV protein into the growing nucleoprotein rod over the range of initial 20S:4S protein mass ratios from 93:7 to 18:82. The results show that the amount of incorporation of 20S TMV protein depends on the initial 20S:4S mass ratio between approximately 100% and 60% 20S protein but that reconstitution can proceed with approximately 100% 20S TMV protein to form full virus-size rods. However, when the initial protein solutions have less than 60% 20S protein, approximately 80% of the reconstituted nucleoprotein is preferentially formed from 4S coat protein. The remaining approximately 20% appears to require preformed 20S coat protein. These results suggest that a larger region of RNA than previously estimated is involved in the rate-limiting nucleation step in assembly and may explain previously conflicting results concerning the elongation phase of assembly when starting with partially assembled rods.

References

  1. Proc Natl Acad Sci U S A. 1955 Oct 15;41(10):690-8 - PubMed
  2. Adv Protein Chem. 1963;18:37-121 - PubMed
  3. Biophys J. 1980 Oct;32(1):313-29 - PubMed
  4. Biophys J. 1980 Oct;32(1):295-312 - PubMed
  5. Philos Trans R Soc Lond B Biol Sci. 1976 Nov 30;276(943):151-63 - PubMed
  6. J Mol Biol. 1979 Feb 5;127(4):487-506 - PubMed
  7. Eur J Biochem. 1979 Jan 2;93(1):157-64 - PubMed
  8. Nucleic Acids Res. 1979 Apr;6(4):1287-308 - PubMed
  9. Adv Protein Chem. 1977;31:187-251 - PubMed
  10. Proc Natl Acad Sci U S A. 1979 Jun;76(6):2745-9 - PubMed
  11. Proc Natl Acad Sci U S A. 1978 Apr;75(4):1727-30 - PubMed
  12. Proc Natl Acad Sci U S A. 1977 Jan;74(1):149-53 - PubMed
  13. Nature. 1977 May 19;267(5608):216-21 - PubMed

Publication Types