Summary
A strain of E. coli K12 has been isolated which gives rise to mutations in a large number of ribosomal proteins. Mutant VT, which was derived from A19, shows a novel type of streptomycin dependence and has an altered ribosomal protein S8. Streptomycin-independent isolates from mutant VT contain a great variety of changed proteins on two-dimensional polyacrylamide gels. 120 revertants screened in this way have changes in thirteen 30S proteins and fifteen 50S proteins. Several mutants were found in which additional proteins are present on the ribosome. Further, there is one instance of a ribosomal protein (L1) being absent, and one of apparent doubling of a ribosomal protein (L7/12). The unique properties of mutant VT probably are the result of the altered S8.
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Bjare, U., Gorini, L.: Drug dependence reversed by a ribosomal ambiguity mutation, ram, in Escherichia coli. J. molec. Biol. 57, 423–435 (1971)
Davis, B.D., Mingiolo, E.S.: Mutants of Escherichia coli requiring methionine or vitamin B12. J. Bact. 60, 17–28 (1950)
Garrett, R.A., Möller, S., Spierer, P., Zimmermann, R.A.: Binding of 50S ribosomal subunit proteins to 23S RNA of Escherichia coli. J. molec. Biol. 88, 553–557 (1974)
Hardy, S.J.S., Kurland, C.G., Voynow, P., Mora, G.: The ribosomal proteins of Escherichia coli. I. Purification of the 30S ribosomal proteins. Biochem. 8, 2897–2905 (1969)
Hasenbank, R., Guthrie, C., Stöffler, G., Wittmann, H.G., Rosen, L., Apirion, D.: Electrophoretic and immunological studies on ribosomal proteins of 100 Escherichia coli revertants from streptomycin dependence. Molec. gen. Genet. 127, 1–18 (1973)
Jaskunas, S.R., Nomura, M.: Organization of ribosomal genes in Escherichia coli. Trends in Biochem. Sci. 1, 159–161 (1976)
Kaltschmidt, E., Wittmann, H.G.: Ribosomal Proteins VII. Two-dimensional polyacrylamide gel electrophoresis for fingerprinting of ribosomal proteins. Analyt. Biochem. 36, 401–412 (1970)
Kreider, G., Brownstein, B.L.: A mutation suppressing streptomycin dependence II. An altered protein of the 30S ribosomal subunit. J. molec. Biol. 61, 135–142 (1971)
Lennox, E.S.:Transduction of linked genetic characters of the host by bacteriophage P1. Virol. 1, 190–206 (1955)
Lelong, J.C., Gros, D., Gros, F., Bollen, A., Maschler, R., Stöffler, G.: Function of individual 30S subunit proteins of Escherichia coli. The effect of specific immunoglobulin fragments (Fab) on the activities of ribosomal decoding sites. Proc. nat. Acad. Sci. (Wash.) 71, 248–252 (1974)
Mizushima, S., Nomura, M.: Assembly mapping of 30S ribosomal proteins from Escherichia coli. Nature (Lond.) 226, 1214–1218 (1970)
Nashimoto, H., Nomura, M.: Structure and function of bacterial ribosomes XI. Dependence of 50S ribosomal assembly on simulatenous assembly of 30S subunits. Proc. nat. Acad. Sci. (Wash.) 67, 1440–1447 (1970)
Saltzman, L., Apirion, D.: Binding of erythromycin to the 50S ribosomal subunit is affected by alterations in the 30S ribosomal subunit. Molec gen. Genet. 143, 301–306 (1976)
Wittmann, H.G., Wittmann-Liebold, B.: Chemical structure of bacterial ribosomal proteins. In: Ribosomes (Nomura, M., Tissières, A., Lengyel, P., eds.). Cold Spr. Harb. Lab. Monogr. Series, 115–160 (1974)
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Communicated by E. Bautz
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Dabbs, E.R., Wittmann, H.G. A strain of Escherichia coli which gives rise to mutations in a large number of ribosomal proteins. Molec. Gen. Genet. 149, 303–309 (1976). https://doi.org/10.1007/BF00268532
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DOI: https://doi.org/10.1007/BF00268532