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Molecular and General Genetics MGG

, Volume 177, Issue 4, pp 645–651 | Cite as

Ribosomal protein modification in Escherichia coli

II. Studies of a mutant lacking the N-terminal acetylation of protein S18
  • Katsumi Isono
  • Setsuko Isono
Article

Summary

A mutant of Escherichia coli K12 has been isolated which shows an alteration in the ribosomal protein S18. Genetic analyses have revealed that the mutation causing this alteration maps at 99.3 min of the E. coli genetic map, between dnaC and deo. This indicated that the mutation has occurred in a gene different from the structural gene for this protein which has been located at 94 min. From the N-terminal amino acid sequence analysis it is concluded that the mutation has resulted in loss of the N-terminal acetyl group of this protein. The gene which is affected in this mutant is termed rimI that most likely specifies an enzyme acetylating the N-terminal alanine of protein S18. The mutation does not affect the acetylation of two other ribosomal proteins, S5 and L12, both of which are known to be acetylated in wild-type E. coli K12.

Keywords

Enzyme Amino Acid Sequence Sequence Analysis Alanine Genetic Analysis 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag 1980

Authors and Affiliations

  • Katsumi Isono
    • 1
  • Setsuko Isono
    • 1
  1. 1.Abt. WittmannMax-Planck-Institut für Molekulare GenetikBerlin 33

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