Summary
The technique of polyacrylamide gel electrophoresis was applied to demonstrate interaction between proteins of different strains of tobacco mosaic virus. The advantages and limitations of the method for such studies have been indicated. The results are discussed in connection with the role of primary structure of TMV-proteins for mixed aggregations.
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Aronsson, T., and A. Grönvall: Scand. J. clin. Lab. Invest. 9, 338 (1957). Cit. by Ch. Wunderly, in: Die Papierelektrophorese, 2nd ed. Frankfurt 1959.
Banerjee, K., and M. A. Lauffer: Polymerization-depolymerization of tobacco mosaic virus protein. VI. Osmotic pressure studies of early stages of polymerization. Biochemistry 5, 1957–1964 (1966).
Caspar, D. L. D.: Assembly and stability of the tobacco mosaic virus particle. Advanc. Protein Chem. 18, 37–121 (1963).
Epstein, C. J.: Relation of protein evolution to tertiary structure. Nature (Lond.) 203, 1350–1352 (1964).
Hannig, K., W. Klofat u. H. Endres: Versuche zur präparativen Isolierung pflanzlicher Zellorganellen mittels der trägerfreien, kontinuierlichen Ablenkungselektrophorese. Z. Naturforsch. 19 b, 1072–1075 (1964).
Melchers, G., G. Schramm, H. Trurnit u. H. Friedrich-Freksa: Die biologische, chemische und elektronenmikroskopische Untersuchung eines Mosaikvirus aus Tomaten. Biol. Zbl. 60, 524–556 (1940).
Rentschler, L.: Aminosäuresequenzen und physikochemisches Verhalten des Hüllproteins eines Wildstammes des Tabakmosaikvirus. II. Aggregationsverhalten und Ladungsverteilung im Vergleich zu den Stämmen vulgare und dahlemense. Molec. Gen. Genetics 100, 96–108 (1967).
Sarkar, S.: Interaction and mixed aggregation of proteins from tobacco mosaic virus strains. Z. Naturforsch. 15 b, 778–786 (1960).
—: Preparation of native tobacco mosaic virus protein by continuous free-flow electrophoresis. Z. Naturforsch. 21 b, 1202–1204 (1966).
—, and H. Jockusch: Wild type and defective coat proteins of tobacco mosaic virus: Electrophoretic analysis of plant extracts in polyacrylamide gels. Biochim. biophys. Acta (Amst.) 106, 259–261 (1968).
Schramm, G.: Über die Spaltung des TMV und die Wiedervereinigung der Spaltstücke zu höhermolekularen Proteinen. I. Die Spaltungsreaktion. Z. Naturforsch. 2 b, 112–121 (1947).
—, u. W. Zillig: Über die Struktur des Tabakmosaikvirus. IV. Die Reaggregation des nukleinsäurefreien Proteins. Z. Naturforsch. 10 b, 493–499 (1955).
Siegel, A., M. Zaitlin, and O. P. Sehgal: The isolation of defective tobacco mosaic virus strains. Proc. nat. Acad. Sci. (Wash.) 48, 1845–1851 (1962).
Tanford, C.: Contribution of hydrophobic interaction to the stability of the globular conformation of proteins. J. Amer. chem. Soc. 84, 4240–4247 (1962).
Tichy, H.: A multisample electrophoresis apparatus using vertical polyacrylamide gel slabs. Analyt. Biochem. 17, 320–326 (1966).
Wittmann, H. G.: Die Proteinstruktur der Defektmutante PM2 des Tabakmosaikvirus. Z. Vererbungsl. 97, 297–304 (1965).
Wittmann-Liebold, B., and H. G. Wittmann: Coat proteins of strains of two RNA viruses: Comparison of their amino acid sequences. Molec. Gen. Genetics 100, 358–363 (1967).
Zaitlin, M., and W. R. Ferris: Unusual aggregation of a nonfunctional tobacco mosaic virus protein. Science 143, 1451–1452 (1964).
—, and W. F. McCaughey: Amino acid composition of a nonfunctional TMV-protein. Virology 26, 500–503 (1965).
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Communicated by H. G. Wittmann
The present observations were reported by us under the title, “Mixed Aggregation of Protein Sub-Units of Tobacco Mosaic Virus Mutants: Role of Primary Structure”, during a symposium on Interaction between Subunits of Biological Macromolecules, organized by the International Union of Pure and Applied Biophysics, and held in Cambridge, U.K., from 24–27th June, 1968.
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Sarkar, S., Schilde-Rentschler, L. Interaction of TMV-proteins during electrophoretic separation in polyacrylamide gels. Molec. Gen. Genet. 103, 244–247 (1968). https://doi.org/10.1007/BF00273694
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DOI: https://doi.org/10.1007/BF00273694