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Ribosomal protein in E. coli: Rate of synthesis and pool size at different growth rates

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Summary

Relative rates of ribosomal protein synthesis αr was determined by pulsechase labeling of cell protein followed by isolation of ribosomes by electrophoresis of complete lysates on agarose gels. The agarose gel fractionation of lysates is described in detail. Cells growing in acetate, glucose and enriched glucose media had αr values of 0.09, 0.16, and 0.24, respectively. Estimates of the free pool of ribosomal protein were obtained from the kinetics of pulse-chase labeling of ribosomal particles (including precursor particles) and gave maximal values of 1.1, 2.1, and 3.1% of total ribosomal protein at the three different growth rates. The kinetics indicate that the free concentrations in the cell are not the same for all ribosomal proteins.

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References

  • Adesnik, M., Levinthal, C.: Synthesis and maturation of ribosomal RNA in Escherichia coli. J. molec. Biol. 46, 281–303 (1969)

    Google Scholar 

  • Bennett, P. M., Maaløe, O.: The effects of fusidic acid on growth, ribosome synthesis and RNA metabolism in Escherichia coli. J. molec. Biol. Submitted (1974)

  • Bickle, T. A., Howard, G. A., Traut, R. R.: Ribosome heterogeneity. The nonuniform distribution of specific ribosomal proteins among different functional classes of ribosomes. J. biol. Chem. 248, 4862–4864 (1973)

    Google Scholar 

  • Burgess, R. R.: Separation and characterization of the subunits of ribonucleic acid polymerase. J. biol. Chem. 244, 6168–6176 (1969)

    Google Scholar 

  • Clark, D. J., Maaløe, O.: DNA replication and the division cycle in Escherichia coli. J. molec. Biol. 23, 99–112 (1967)

    Google Scholar 

  • Dahlberg, A. E., Dingman, C. W., Peacock, A. C.: Electrophoretic characterization of bacterial polyribosomes in agarose-acrylamide composite gels. J. molec. Biol. 41, 139–147 (1969)

    Google Scholar 

  • Dahlberg, A. E., Peacock, A. C.: Studies of 16 and 23S ribosomal RNA of Escherichia coli using composite gel electrophoresis. J. molec. Biol. 55, 61–74 (1971)

    Google Scholar 

  • Dennis, P. P., Bremer, H.: The differential rate of ribosomal protein synthesis in Escherichia coli B/r. J. molec. Biol. Submitted (1974)

  • Deusser, E.: Heterogeneity of ribosomal populations in Escherichia coli cells grown in different media. Molec. gen. Genet. 119, 249–258 (1972)

    Google Scholar 

  • Duin, J. van, Knippenberg, P. H. van., Dieben, M., Kurland, C. G.: Functional heterogeneity of the 30S ribosomal subunit of Escherichia coli. II. Effect of S21 on initiation. Molec. gen. Genet. 116, 181–191 (1972)

    Google Scholar 

  • Duin, J. van, Kurland, C. G.: Functional heterogeneity of the 30S ribosomal subunit of E. coli. Molec. gen. Genet. 109, 169–176 (1970)

    Google Scholar 

  • Fairbanks, C., Jr., Levinthal, C., Reeder, R. H.: Analysis of 14C-labeled proteins by disc electrophoresis. Biochem. biophys. Res. Commun. 20, 393–399 (1965)

    Google Scholar 

  • Forchhammer, J., Lindahl, L.: Growth rate of polypeptide chains as a function of the cell growth rate in a mutant of Escherichia coli 15. J. molec. Biol. 55, 563–568 (1971)

    Google Scholar 

  • Gausing, K.: Efficiency of protein and messenger RNA synthesis in bacteriophage T4-infected cells of Escherichia coli. J. molec. Biol. 71, 529–545 (1972)

    Google Scholar 

  • Gierer, L., Gierer, A.: Synthesis of ribosomal proteins and formation of ribosomes in Escherichia coli. J. molec. Biol. 34, 293–303 (1968)

    Google Scholar 

  • Gupta, R. S., Singh, U. N.: Biogenesis of ribosomes: Free ribosomal protein pools in Escherichia coli. J. molec. Biol. 69, 279–301 (1972)

    Google Scholar 

  • Hardy, S. J. S., Kurland, C. G., Voynow, P., Mora, G.: The ribosomal proteins of Escherichia coli. I. Purification of the 30S ribosomal proteins. Biochemistry 8, 2897–2905 (1969)

    Google Scholar 

  • Kurland, C. G., Voynow, P., Hardy, S. J. S., Randall, L., Lutter, L.: Physical and functional heterogeneity of E. coli ribosomes. Cold Spr. Harb. Symp. quant. Biol. 34, 17–24 (1969)

    Google Scholar 

  • Maaløe, O.: An analysis of bacterial growth. Develop. Biol., Suppl. 3, 33–58 (1969)

  • Maaløe, O., Kjeldgaard, N. O.: Control of macromolecular synthesis. New York: W. A. Benjamin, Inc. 1966

    Google Scholar 

  • Marvaldi, J., Pichon, J., Marchis-Mouren, G.: The in vivo order of addition of ribosomal proteins in the course of Escherichia coli 30-S subunit biogenesis. Biochim. biophys. Acta (Amst.) 269, 173–177 (1972)

    Google Scholar 

  • Mora, G., Donner, D., Thammana, P., Lutter, L., Kurland, C. G.: Purification and characterization of 50S ribosomal proteins of Escherichia coli. Molec. gen. Genet. 112, 229–242 (1971)

    Google Scholar 

  • Nath, K., Koch, A. L.: Protein degradation in Escherichia coli. I. Measurement of rapidly and slowly decaying components. J. biol. Chem. 245, 2889–2900 (1970)

    Google Scholar 

  • Nierhaus, K. H., Bordasch, K., Homann, H. E.: Ribosomal proteins. XLIII. In vivo assembly of Escherichia coli ribosomal proteins. J. molec. Biol. 74, 587–597 (1973)

    Google Scholar 

  • Nomura, M.: Assembly of bacterial ribosomes. Science 179, 864–873 (1973)

    Google Scholar 

  • Peacock, A. C., Dingman, C. W.: Molecular weight estimation and separation of ribonucleic acid by electrophoresis in agarose-acrylamide composite gels. Biochemistry 7, 668–674 (1968)

    Google Scholar 

  • Pichon, J., Marvaldi, J., Marchis-Mouren, G.: The in vivo order of addition of ribosomal proteins in the course of E. coli 50S subunit biogenesis. Biochem. biophys. Res. Commun. 47, 531–538 (1972)

    Google Scholar 

  • Raymond, S.: Acrylamide gel electrophoresis. Ann. N.Y. Acad. Sci. 121, 350–365 (1964)

    Google Scholar 

  • Schleif, R.: Control of production of ribosomal protein. J. molec. Biol. 27, 41–55 (1967)

    Google Scholar 

  • Schleif, R. F.: Origin of chloramphenicol particle protein. J. molec. Biol. 37, 119–129 (1968)

    Google Scholar 

  • Sekiguchi, M., Iida, S.: Mutants of Escherichia coli permeable to actinomycin. Proc. nat. Acad. Sci. (Wash.) 58, 2315–2320 (1967)

    Google Scholar 

  • Sells, B. H., Davis, F. C., Jr.: Biogenesis of 50S particles in exponentially growing Escherichia coli. J. molec. Biol. 47, 155–167 (1970)

    Google Scholar 

  • Thammana, P., Kurland, C. G., Deusser, E., Weber, J., Maschler, R., Stöffler, G., Wittmann, H. G.: Structural and functional evidence for a repeated 50S subunit ribosomal protein. Nature (Lond.) New Biol. 242, 47–49 (1973)

    Google Scholar 

  • Tissières, A., Watson, J. D., Schlessinger, D., Hollingworth, B. R.: Ribonucleoprotein particles from Escherichia coli. J. molec. Biol. 1, 221–233 (1959)

    Google Scholar 

  • Traut, R. R., Delius, H., Ahmad-Zadeh, C., Bickle, T. A., Pearson, P., Tissières, A.: Ribosomal proteins of E. coli: Stoichiometry and implications for ribosome structure. Cold Spr. Harb. Symp. quant. Biol. 34, 25–38 (1969)

    Google Scholar 

  • Voynow, P., Kurland, C. G.: Stoichiometry of the 30S ribosomal proteins of Escherichia coli. Biochemistry 10, 517–524 (1971)

    Google Scholar 

  • Waller, J.-P.: The NH2-terminal residues of the proteins from cell-free extracts of E. coli. J. molec. Biol. 7, 483–496 (1963).

    Google Scholar 

  • Weber, H. J.: Stoichiometric measurements of 30S and 50S ribosomal proteins from Escherichia coli. Molec. gen. Genet. 119, 233–248 (1972)

    Google Scholar 

  • Zimmermann, R. A., Muto, A., Fellner, P., Ehresmann, C., Branlant, C.: Location of ribosomal protein binding sites on 16S ribosomal RNA. Proc. nat. Acad. Sci. (Wash.) 69, 1282–1286 (1972)

    Google Scholar 

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  1. University Institute of Microbiology, Copenhagen, Denmark

    Kirsten Gausing

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  1. Kirsten Gausing
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Communicated by H. G. Wittmann

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Gausing, K. Ribosomal protein in E. coli: Rate of synthesis and pool size at different growth rates. Molec. Gen. Genet. 129, 61–75 (1974). https://doi.org/10.1007/BF00269266

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