Mechanism of Action of Bottromycin in Polypeptide Biosynthesis

J-STAGE
  • LIN YONG-CHI
    the Institute of Applied Microbiology, University of Tokyo
  • TANAKA NOBUO
    the Institute of Applied Microbiology, University of Tokyo

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Description

The poly UC- or poly UG-directed incorporation of phenylalanine, proline, leucine, serine and valine into polypeptide was inhibited by bottromycin A2 and its hydrazide. The formation of a ternary complex between the ribosomes, poly C and prolyl-sRNA was not significantly affected by bottromycin A2 or its hydrazide. Bottromycin did not cause significant peptide release nor inhibit puromycin-dependent release of polyproline from ribosomes. The activity of bottromycin A2 was reversed by a high concentration of ribosomes but not by that of the 105, 000×g supernatant or poly C. The binding of chloramphenicol to the ribosomes was not antagonized by bottromycin A2 or its hydrazide. The inhibitory activity of bottromycin A2 seemed to be reversible, because the effect of the antibiotic on the ribosomes or supernatant was lost on dialysis.

Journal

  • J Biochem (Tokyo)

    J Biochem (Tokyo) 63 (1), 1-7, 1968

    The Japanese Biochemical Society

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