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Zeitschrift für Vererbungslehre

, Volume 94, Issue 4, pp 427–435 | Cite as

Die primäre Proteinstruktur von Stämmen des Tabakmosaikvirus

Aminosäuresequenzen des Proteins des TabakmosaikvirusstammesDahlemense Teil III Diskussion der Ergebnisse
  • B. Wittmann-Liebold
  • H. G. Wittmann
Article

Summary

In contrast to chemically induced mutants of tobacco mosaic virus (TMV) in which we have found replacement of one or at most of two amino acids per coat protein chain, the protein chains of naturally occurring TMV strains differ from each other in numerous positions. The complete amino acid sequence of the naturally occurring TMV straindahlemense isolated byMelchers (1940) has been determined. It differs in 30 of the 158 amino acid positions from the TMV wild strainvulgare (Fig. 1). This is the first case in which complete amino acid sequences of the coat proteins of two virus strains can be compared. Such a comparison permits conclusions about the structure of the protein subunits and about certain aspects of the genetic code to be drawn.

The electrophoretic mobility curves for the virus rods and the A proteins ofvulgare anddahlemense (Fig. 4) can be explained on the basis of the amino acid sequences of the two strains. Spatial distribution of the positive and negative groups within the protein subunits are discussed. One particular segment of the protein chain appears to be so important for the secondary and/or tertiary structure of the protein subunit that amino acid replacements within this segment in general lead to a loss of infectivity.

The 46 cases in which we have exactly located the positions of amino acid differences betweenvulgare and various TMV mutants and strains are summarized in Table 1. Combination of the data in Table 1 with the base compositions of the triplets as obtained from the cell free system ofE. coli permits conclusions about the nucleotide sequence within the triplets to be drawn. The triplets shown in Table 2 represent, at present, the best agreement between the data from the cell free system and the work with TMV mutants.

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Literatur

  1. Anderer, F. A.: Die Reihenfolge der Aminosäuren im Protein des Tabakmosaikvirus. Z. Naturforsch.17b, 526–543 (1962).Google Scholar
  2. Anderer, F. A., H. Uhlig, E. Weber andG. Schramm: Primary structure of the protein of tobacco mosaic virus. Nature (Lond.)186, 922–925 (1960).Google Scholar
  3. Benzer, S., andS. W. Champe: A change from nonsense to sense in the genetic code. Proc. nat. Acad. Sci. (Wash.)48, 1114–1121 (1962).Google Scholar
  4. Crick, F. H. C., L. Barnett, S. Brenner andR. J. Watts-Tobin: General nature of the genetic code for proteins. Nature (Lond.)192, 1227–1232 (1961).Google Scholar
  5. Ehrenstein, G. v., andF. Gonano: Degenerate transfer RNAs as amino adaptors in protein synthesis. Cold Spr. Harb. Symp. quant. Biol.28 (im Druck).Google Scholar
  6. Hanada, M., andD. L. Rucknagel: The abnormality of the primary structure of haemoglobin Shimonoseki. Biochem. biophys. Res. Commun.11, 229–234 (1963).Google Scholar
  7. Jones, O. W., andM. W. Nirenberg: Qualitative survey of RNA codewords. Proc. nat. Acad. Sci. (Wash.)48, 2115–2123 (1962).Google Scholar
  8. Jukes, T. H.: Observations on the possible nature of the genetic code. Biochem. biophys. Res. Commun.10, 155–159 (1963a).Google Scholar
  9. —: The genetic code. Amer. Sci.51, 227–245 (1963b).Google Scholar
  10. Knight, C. A.: Chemistry of viruses. In: Protoplasmatologia, vol. IV, 177 p. Wien: Springer 1963.Google Scholar
  11. —,D. M. Silva, D. Dahl andA. Tsugita: Two distinctive strains of tobacco mosaic virus. Virology16, 236–243 (1962).Google Scholar
  12. Kramer, E., u.H. G. Wittmann: Elektrophoretische Untersuchungen der A-Proteine dreier Tabakmosaikvirusstämme. Z. Naturforsch.13b, 30–33 (1958).Google Scholar
  13. Melchers, G.: Die biologische Untersuchung des “Tomatenvirus Dahlem 1940”. Biol. Zbl.60, 527–537 (1940).Google Scholar
  14. Nirenberg, M. W., andJ. H. Matthaei: The dependence of cell free protein synthesis inE. coli upon naturally occurring or synthetic poly-ribonucleotides. Proc. nat. Acad. Sci. (Wash.)47, 1588–1602 (1961).Google Scholar
  15. Schramm, G.: Die Reindarstellung und die chemischen Eigenschaften des “Tomatenmosaikvirus Dahlem 1940”. Biol. Zbl.60, 538–546 (1940).Google Scholar
  16. Sueoka, N., andT. Yamane: Fractionation on amino acyl acceptor RNA on a methylated albumin column. Proc. nat. Acad. Sci. (Wash.)48, 1454–1461 (1962).Google Scholar
  17. Tsugita, A.: The proteins of mutants of TMV. J. molec. Biol.5, 284–300 (1962).Google Scholar
  18. —, andH. Fraenkel-Conrat: The amino acid composition and C-terminal sequence of a chemically evoked mutant of TMV. Proc. nat. Acad. Sci. (Wash.)46, 636–642 (1960).Google Scholar
  19. ——: The composition of proteins of chemically evoked mutants of TMV-RNA. J. molec. Biol.4, 73–82 (1962).Google Scholar
  20. D. T. Gish, J. Young, H. Fraenkel-Conrat, C. A. Knight andW. M. Stanley: The complete amino acid sequence of the protein of tobacco mosaic virus. Proc. nat. Acad. Sci. (Wash.)46, 1436–1469 (1960).Google Scholar
  21. Wahba, A. J., C. Basilio, J. F. Speyer, P. Lengyel, R. S. Miller andS. Ochoa: Synthetic polynucleotides and the amino acid code. V. Proc. nat. Acad. Sci. (Wash.)48, 1683–1686 (1962).Google Scholar
  22. R. S. Miller, C. Basilio, R. S. Gardner, P. Lengyel andJ. F. Speyer: Synthetic polynucleotides and the amino acid code. IX. Proc. nat. Acad. Sci. (Wash.)49, 880–885 (1963).Google Scholar
  23. Weisblum, B., S. Benzer andR. W. Holley: A physical basis for the degeneracy in the amino acid code. Proc. nat. Acad. Sci. (Wash.)48, 1449–1454 (1962).Google Scholar
  24. Wittmann, H. G.: Vergleich der Proteine des Normalstamms und einer Nitritmutante des TMV. Z. Vererb.-Lehre90, 463–475 (1959).Google Scholar
  25. Wittmann, H. G.: Studies on the nucleic acid-protein correlation in tobacco mosaic virus. Proc. V. Internat. Congr. Biochem., Moscow1961, vol. I, pp. 240–254.Google Scholar
  26. —: Proteinuntersuchungen an Mutanten des Tabakmosaikvirus als Beitrag zum Problem des genetischen Codes. Z. Vererb.-Lehre93, 491–530 (1962).Google Scholar
  27. Wittmann, H. G., andB. Wittmann-Liebold: Tobacco mosaic virus mutants and the genetic coding problem. Cold Spr. Harb. Symp. quant. Biol.28 (im Druck).Google Scholar
  28. Wittmann-Liebold, B., andH. G. Wittmann: Die primäre Proteinstruktur von Stämmen des Tabakmosaikvirus: Teil I. Hoppe-Seylers Z. physiol. Chem. (im Druck) (1963a).Google Scholar
  29. Wittmann-Liebold, B., andH. G. Wittmann: Die primäre Proteinstruktur von Stämmen des Tabakmosaikvirus: Teil II. Z. Naturforsch. (im Druck) (1963b).Google Scholar

Copyright information

© Springer-Verlag 1963

Authors and Affiliations

  • B. Wittmann-Liebold
    • 1
  • H. G. Wittmann
    • 1
  1. 1.Abt. MelchersMax-Planck-Institut für BiologieTübingen/N

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