Skip to main content
Biophysical Journal logoLink to Biophysical Journal
. 1968 Mar;8(3):380–388. doi: 10.1016/S0006-3495(68)86494-X

Effect of Chemicals on the Early Stages of Tobacco Mosaic Virus Protein Polymerization

Ragaa A Shalaby
PMCID: PMC1367342  PMID: 4997647

Abstract

Osmotic pressure and sedimentation velocity techniques have been used to investigate the effect of KSCN, thiourea, EDTA, acetamide, and sucrose on the 53,000 molecular weight A protein at pH 6.5-7.0. In the presence of all the compounds except thiocyanate, the number average molecular weight lies between 50,000 and 56,000 which corresponds to a trimer of three chemical subunits. In the presence of thiocyanate, the molecular weight decreases initially sharply with increasing concentration of thiocyanate to 0.1 M, then dissociation proceeds with less efficiency with increasing concentration of KSCN until a molecular weight close to a monomer (21,700) is obtained at 0.59 M KSCN. Sedimentation data agree with osmotic pressure data since, in the absence of thiocyanate, the measured values of S20,w indicate that the favored state is that of a trimer. In the presence of thiocyanate, however, S20,w decreases with thiocyanate concentration to S20,w = 1.9, which is the value reported for the monomer.

Full text

PDF
380

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ANSEVIN A. T., LAUFFER M. A. Native tobacco mosaic virus protein of molecular weight 18,000. Nature. 1959 Jun 6;183(4675):1601–1602. doi: 10.1038/1831601b0. [DOI] [PubMed] [Google Scholar]
  2. Banerjee K., Lauffer M. A. Polymerization--depolymerization of tobacco mosaic virus protein. VI. Osmotic pressure studies of early stages of polymerization. Biochemistry. 1966 Jun;5(6):1957–1964. doi: 10.1021/bi00870a024. [DOI] [PubMed] [Google Scholar]
  3. Fraenkel-Conrat H., Williams R. C. RECONSTITUTION OF ACTIVE TOBACCO MOSAIC VIRUS FROM ITS INACTIVE PROTEIN AND NUCLEIC ACID COMPONENTS. Proc Natl Acad Sci U S A. 1955 Oct 15;41(10):690–698. doi: 10.1073/pnas.41.10.690. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. GINOZA W., ATKINSON D. E., WILDMAN S. G. A differential ability of strains of tobacco mosaic virus to bind host-cell nucleoprotein. Science. 1954 Feb 26;119(3087):269–271. doi: 10.1126/science.119.3087.269. [DOI] [PubMed] [Google Scholar]
  5. LAUFFER M. A., ANSEVIN A. T., CARTWRIGHT T. E., BRINTON C. C., Jr Polymerization-depolymerization of tobacco mosaic virus protein. Nature. 1958 May 10;181(4619):1338–1339. doi: 10.1038/1811338b0. [DOI] [PubMed] [Google Scholar]
  6. Lauffer M. A. Polymerization-depolymerization of tobacco mosaic virus protein. VII. A model. Biochemistry. 1966 Jul;5(7):2440–2446. doi: 10.1021/bi00871a038. [DOI] [PubMed] [Google Scholar]
  7. Scheele R. B., Lauffer M. A. Acid-base titrations of tobacco mosaic virus and tobacco mosaic virus protein. Biochemistry. 1967 Oct;6(10):3076–3081. doi: 10.1021/bi00862a014. [DOI] [PubMed] [Google Scholar]
  8. Shalaby R. A., Lauffer M. A. Polymerization-depolymerization of tobacco mosaic virus protein. IX. Effect of various chemicals. Biochemistry. 1967 Aug;6(8):2465–2473. doi: 10.1021/bi00860a024. [DOI] [PubMed] [Google Scholar]
  9. TONOMURA Y., SEKIYA K., IMAMURA K. The optical rotatory dispersion of myosin A. I. Effect of inorganic salt. J Biol Chem. 1962 Oct;237:3110–3115. [PubMed] [Google Scholar]
  10. WITTMANN H. G., BRAUNITZER G. Isolation and composition of all tryptic peptides of TMV. Virology. 1959 Dec;9:726–728. doi: 10.1016/0042-6822(59)90170-9. [DOI] [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES