RALyase; a terminator of elongation function of depurinated ribosomes

FEBS Letters

Ozawa, Akihiko²  Endo, Yaeta²  Takai, Kazuyuki²  Uchiumi, Toshio¹  Hori, Hiroyuki²  Sawasaki, Tatsuya² 

[1] The Institute of High Polymer Research, Faculty of Textile Science and Technology, Shinshu University, Ueda 386-8567, Japan;Department of Applied Chemistry, Faculty of Engineering, Ehime University, Matsuyama 790-8577, Japan

关键词: RALyase;    Cell-free protein synthesis system;    Poly(Phe) synthesis;    GTPase;    Sarcin–ricin loop;    Ribosome-inactivating protein;   

DOI  :  10.1016/S0014-5793(03)01304-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Plant ribosomal RNA apurinic site specific lyase (RALyase) cleaves the phosphodiester bond at the depurinated site produced by ribosome-inactivating protein, while the biological role of this enzyme is not clear. As the depurinated ribosomes retain weak translation elongation activities, it was suggested that RALyase completes the ribosome inactivation. To confirm this point, we measured the effects of the phosphodiester cleavage using a fusion of wheat RALyase produced with a cell-free protein synthesis system from wheat germ. The results indicated that RALyase diminishes the residual elongation activities of the depurinated ribosomes.

【 授权许可】

Unknown