Adaptability of nonnatural aromatic amino acids to the active center of the E. coli ribosomal A site

FEBS Letters

Sisido, Masahiko¹  Takai, Kazuyuki²  Yokoyama, Shigeyuki²  Hohsaka, Takahiro¹  Sato, Ken¹ 

[1] Research Laboratory of Resources Utilization, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 227, Japan;Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, Japan

关键词: Nonnatural amino acid;    Puromycin;    Protein biosynthesis;    Ribosome;    A site;   

DOI  :  10.1016/0014-5793(93)80436-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

3'-N-Aminoacyl analogs of puromycin with nonnatural aromatic amino acids were synthesized and their inhibitory activity in E.coli in vitro protein synthesizing system was evaluated. The analogs with l-2-naphthylalanine, l-p-biphenylalanine, l-2-anthrylalanine and trans-l-p-phenylazophenylalanine were found to inhibit the protein synthesis with high efficiency. The inhibition suggests that these nonnatural amino acids are accepted by the active center of the E. coli ribosomal A site. A model for the adaptability of nonnatural aromatic amino acids to the active center is proposed.

【 授权许可】

Unknown