Summary
Ribosomes were isolated from larvae and adult flies, and the purity of the preparation was checked by electron microscopy. The ribosomal proteins were extracted with cold dilute hydrochloric acid, and precipitated with cold acetone. The proteins were characterized by polyacrylamide gel electrophoresis. At pH 3.0 at least 25 bands of different color intensities were resolved, forming a complex pattern.
On the basis of electrophoretic mobilities, it was shown that some ribosomal proteins are species-specific, and that larval ribosomes have three protein components more than ribosomes from adult flies.
Incubation of the ribosomes with 0.75 M NH4Cl at a low Mg++ concentration lead to detachment of 64% of the ribosomal protein. This detachment of protein molecules was considerably reduced by a five-fold increase of Mg++ ions.
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References
Allen, R. J. L.: The estimation of phosphorus. Biochem. J. 34, 858–865 (1940).
Atsmon, A., Spitnik-Elson, P., Elson, D.: Detachment of ribosomal proteins by salt. II. Some properties of proteindeficient particles formed by the detachment of ribosomal proteins. J. molec. Biol. 45, 125–135 (1969).
Bielka, H., Welfle, H.: Characterization of ribosomal proteins from different tissues and species of animals by electrophoresis on polyacrylamide gel. Molec. Gen. Genetics 102, 128–131 (1968).
Craven, G. R., Voynow, P., Hardy, S. J. S., Kurland, C. G.: The ribosomal proteins of Escherichia coli. II. Chemical and physical characterization of the 30 s ribosomal proteins. Biochemistry 8, 2906–2915 (1969).
Hardy, S. J. S., Kurland, C. G., Voynow, P., Mora, G.: The ribosomal proteins of Escherichia coli. I. Purification of the 30 s ribosomal proteins. Biochemistry 8, 2897–2905 (1969).
Hosokawa, K., Fujimura, R. K., Nomura, M.: Reconstitution of functionally active ribosomes from inactive subparticles and proteins. Proc. nat. Acad. Sci. (Wash.) 55, 198–204 (1966).
Itoh, T., Otaka, E., Osawa, S.: Release of ribosomal proteins from Escherichia coli ribosomes with high concentrations of lithium chloride. J. molec. Biol. 33, 109–122 (1968).
Kaltschmidt, E., Rudloff, V., Stöffler, G., Chersi, A., Dzionara, M., Donner, D., Wittmann, H. G.: Ribosomal proteins of Escherichia coli and yeast. 4. Wissenschaftliche Konferenz der Ges. Dtsch. Naturforscher und Ärzte Berlin 1967, Symposium on Molecular Genetics, S. 6–25. Berlin-Heidelberg-New York: Springer 1960.
Leboy, P. S., Cox, E. C., Flaks, J. G.: The chromosomal site specifying a ribosomal protein in Escherichia coli. Proc. nat. Acad. Sci. (Wash.) 52, 1367–1374 (1964).
Low, R. B., Wool, I. G.: Mammalian ribosomal proteins: Analysis by electrophoresis on polyacrylamide gel. Science 155, 330–332 (1967).
Lowry, O. H., Rosebrough, N. J., Farr, A. L., Randall, R. J.: Protein measurement with the Folin phenol reagent. J. biol. Chem. 193, 265–275 (1951).
Luft, J. H.: Improvements in epoxy resin embedding methods. J. biophys. biochem. Cytol. 9, 409–414 (1961).
Mundell, R. D.: Studies on nucleolar and ribosomal basic proteins and their relationship to nucleolar function. Exp. Cell Res. 53, 395–400 (1968).
Nomura, M., Traub, P.: Structure and function of Escherichia coli, ribosomes. III. Stoichiometry and rate of the reconstitution of ribosomes from subribosomal particles and split proteins. J. molec. Biol. 34, 609–619 (1968).
Ozaki, M., Mizushima, S., Nomura, M.: Identification and functional characterization of the protein controlled by the streptomycin-resistent locus in Escherichia coli. Nature (Lond.) 222, 333–339 (1969).
Panyim, S., Chalkley, R.: High resolution acrylamide gel electrophoresis of histones. Arch. Biochem. Biophys. 130, 337–346 (1969).
Reisfeld, R. A., Lewis, U. J., Williams, D. E.: Disc electrophoresis of basic proteins and peptides on polyacrylamide gels. Nature (Lond.) 195, 281–283 (1962).
Spirin, A. S., Gavrilova, L. P.: Molec. biol. boochem. and biophys. 4. The ribosome, p. 36–37, p. 71–74. Berlin-Heidelberg-New York: Springer 1969.
Spitnik-Elson, P., Atsmon, A.: Detachment of ribosomal proteins by salt. I. Effect of conditions on the amount of protein detached. J. molec. Biol. 45, 113–124 (1969).
Traub, P., Hosokawa, K., Craven, G. R., Nomura, M.: Structure and function of Escherichia coli ribosomes. IV. Isolation and characterization of functionally active ribosomal proteins. Proc. nat. Acad. Sci. (Wash.) 58, 2430–2436 (1967).
— Nomura, M.: Streptomycin sensitivity and the structural components of the 30 s ribosomes of Escherichia coli. J. molec. Biol. 19, 211–214 (1966a).
— Nomura, M.: Structure and function of Escherichia coli ribosomes. I. Partial fractionation of the functionally active ribosomal proteins and reconstitution of artificial subribosomal particles. J. molec. Biol. 34, 575–593 (1968a).
—: Structure and function of Escherichia coli ribosomes. V. Reconstitution of functionally active 30 s ribosomal particles from RNA and proteins. Proc. nat. Acad. Sci. (Wash.) 59, 777–784 (1968c).
— Tu, L.: Physical and functional heterogeneity of ribosomal proteins. J. molec. Biol. 19, 215–218 (1966b).
—, Söll, D., Nomura, M.: Structure and function of Escherichia coli ribosomes. II. Translational fidelity and efficiency in protein synthesis of a protein-deficient subribosomal particle. J. molec. Biol. 34, 595–608 (1968b).
Waller, J. P.: Fractionation of the ribosomal protein from Escherichia coli. J. molec. Biol. 10, 319–336 (1964).
—, Harris, J. I.: Studies on the composition of the protein from Escherichia coli ribosomes. Proc. nat. Acad. Sci. (Wash.) 57, 18–23 (1961).
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Communicated by H. G. Wittmann
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Lambertsson, A.G., Rasmuson, S.B. & Bloom, G.D. The ribosomal proteins of Drosophila melanogaster . Molec. Gen. Genet. 108, 349–357 (1970). https://doi.org/10.1007/BF00267772
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DOI: https://doi.org/10.1007/BF00267772