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Ribosomal protein modification in Escherichia coli

III. Studies of mutants lacking an acetylase activity apecific for protein L12


Among mutants of E. coli selected for temperaturesensitive growth, four were found to possess alterations in ribosomal proteins L7/L12. Of these, three apparently lack protein L7, the acetylated form of protein L12. Genetic analyses have revealed that the mutation responsible for this alteration maps at a locus around 34 min of the current E. coli genetic map, which is clearly different from the location for the structural gene for protein L7/L12 which is situated at 89 min. Hence, the gene affected in these mutants was termed rimL. Tryptic and thermolysin fingerprints of the protein L12 purified from the rimL mutants showed a profile indistinguishable from that of wild-type protein. It was found that the acetylase activity specific for protein L12 was negligible, when assayed in vitro, in the high-speed supernatant prepared from mutant cells. These results indicated that the three mutants contain mutations in the gene rimL that codes for an acetylating enzyme specific for ribosomal protein L12.

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Correspondence to Katsumi Isono.

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Previous paper in this series is Isono and Isono (1980)

Communicated by A. Böck

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Isono, S., Isono, K. Ribosomal protein modification in Escherichia coli . Molec. Gen. Genet. 183, 473–477 (1981).

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  • Enzyme
  • Genetic Analysis
  • Structural Gene
  • Ribosomal Protein
  • Mutant Cell