Mode of action of bottromycin A2: Effect of bottromycin A2 on polysomes

FEBS Letters

Kaji, Akira¹  Otaka, Tadahiko¹ 

[1] Department of Microbiology, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA

关键词: Bottromycin;    Polysomes;    Acceptor site;    Protein synthesis;    Aminoacyl tRNA release;    EFG;    elongation factor G;    DTT;    dithiothreitol;    Tris;    Tris-(hydroxymethyl) aminomethane;    EFTu;    elongation factor Tu;   

DOI  :  10.1016/0014-5793(83)80118-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

When bottromycin A₂ was added to an in vitro protein synthesis system carried out by naturally occurring polysomes, it inhibited protein synthesis effectively. Examination of the 3 steps of peptide chain elongation revealed that the binding of aminoacyl-tRNA to the polyribosomes was inhibited by bottromycin A₂. In contrast, we concluded that the peptide bond formation and the translocation steps in this system were not inhibited by bottromycin A₂ on the basis of the following observation: (1) the break-down of polysomes, which is dependent of EFG, puromycin and RR (ribosome releasing) factor, was insensitive to bottromycin A₂; (2) the puromycin dependent release of polypeptide from polysomes, with or without EFG, was not inhibited by bottromycin A₂. Thus bottromycin specifically interferes with proper functioning of the A sites of polysomes. This is consistent with results obtained using the model system with synthetic polynucleotides.

【 授权许可】

Unknown