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Studies on the interaction between ribosomes and14CH3−F3 initation factor

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Summary

Initiation factor F3 has been purified fromEscherichia coli and labelledin vitro by reductive alkylation. The14CH3−F3 so obtained had a specific activity of about 1 000 cpm/μg and was shown to have retained its biological activity. Labelled F3 binds to 30S ribosomal subunits ofEscherichia coli andBacillus stearothermophilus, but does not bind to either 70S ribosomes or 50S ribosomal subunits. The stoichiometry of the binding indicates that one molecule of14CH3−F3 is bound to each 30S ribosomal subunit. Several antibiotics, known to interact with 30S subunits, inhibit the binding. Functional studies indicate that F3 is released from 30S ribosomes as a result of the formation of the “70S initiation complex”.

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References

  • Berissi, H., Groner, Y., Revel, M.: Effect of purified initiation factor F3 (B) in the selection of ribosomal binding sites on phage MS2 RNA. Nature New Biol.234, 44–47 (1971).

    Google Scholar 

  • Davis, B. D.: Role of subunits in the ribosome cycle. Nature (Lond.)231, 153–157 (1971).

    Google Scholar 

  • Dubnoff, J. S., Maitra, U.: Isolation and properties of polypeptide chain initiation factor FII fromEscherichia coli: evidence for a dual function. Proc. nat. Acad. Sci. (Wash.)68, 318–323 (1971).

    Google Scholar 

  • Friedman, S. M.: Protein-synthesizing machinery of thermophilic bacteria. Bact. Rev.32, 27–38 (1968).

    Google Scholar 

  • Gualerzi, C., Pon, C. L., Kaji, A.: Initiation factor dependent release of aminoacyl-tRNAs from complexes of 30S ribosomal subunits, synthetic polynucleotide and aminoacyl-tRNA. Biochem. biophys. Res. Commun.45, 1312–1319 (1971).

    Google Scholar 

  • Iwasaki, K., Sabol, S., Wahba, A. J., Ochoa, S.: Translation of the genetic message. VII Role of initiation factors in formation of the chain initiation complex withEscherichia coli ribosomes. Arch. Biochem. Biophys.125, 542–547 (1968).

    Google Scholar 

  • Kaempfer, R.: Control of single ribosome formation by an initiation factor for protein synthesis. Proc. nat. Acad. Sci. (Wash.)68, 2458–2462 (1971).

    Google Scholar 

  • Lee-Huang, S., Ochoa, S.: Messenger discriminating species of initiation factor F3. Nature New Biol.234, 236–239 (1971).

    Google Scholar 

  • Lodish, H. F.: Specificity in bacterial protein synthesis: Role of initiation factors and ribosomal subunits. Nature (Lond.)226, 705–707 (1970).

    Google Scholar 

  • 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).

    Google Scholar 

  • Pestka, S.: Inhibitors of ribosome functions. Ann. Rev. Microbiol.25, 487–562 (1971).

    Google Scholar 

  • Revel, M., Greenshpan, H.: Specificity in the binding ofEscherichia coli ribosomes to natural messenger RNA. Europ. J. Biochem.16, 117–122 (1970).

    Google Scholar 

  • Revel, M., Lelong, J. C., Brawerman, G., Gros, F.: Function of three protein factors and ribosomal subunits in the initiation of protein synthesis inEscherichia coli. Nature (Lond.)219, 1016–1021 (1968).

    Google Scholar 

  • Rice, R. H., Means, G. E.: Radioactive labeling of proteinsin vitro. J. biol. Chem.246, 831–832 (1971).

    Google Scholar 

  • Sabol, S., Ochoa, S.: Ribosomal binding of labelled initiation factor F3. Nature New Biol.234, 233–236 (1971).

    Google Scholar 

  • Sabol, S., Sillero, M. A. G., Iwasaki, K., Ochoa, S.: Purification and properties of initiation factor F3. Nature (Lond.)228, 1269–1273 (1970).

    Google Scholar 

  • Vermeer, C., Talens, J., Bloemsma-Jonkman, F., Bosch, L.: Studies on the ribosomal initiation factor F3. Multiplicity of F3 and DF activities. FEBS Letters19, 201–206 (1971).

    Google Scholar 

  • Vogel, Z., Vogel, T., Zamir, A., Elson, D.: The protection by 70S ribosomes of N-Acyl-aminoacyl-tRNA against cleavage by peptidyl-tRNA hydrolase and its use to assay ribosomal association. Europ. J. Biochem.21, 582–592 (1971).

    Google Scholar 

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Communicated by H. G. Wittmann

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Pon, C.L., Friedman, S.M. & Gualerzi, C. Studies on the interaction between ribosomes and14CH3−F3 initation factor. Molec. gen. Genet. 116, 192–198 (1972). https://doi.org/10.1007/BF00582228

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