Inactivation of oncoprotein binding by a single Cys706‐to‐Tyr substitution in the retinoblastoma protein

FEBS Letters

Sasaki, Masao S.²  Taya, Yoichi¹  Kato, Mitsuo V.²  Saijo, Masafumi¹  Ishizaki, Kanji² 

[1] Biology Division, National Cancer Center Research Institute, Tsukiji, Chuo-ku, Tokyo 104, Japan;Radiation Biology Center, Kyoto University, Yoshida-konoecho, Sakyo-ku, Kyoto 606, Japan

关键词: Retinoblastoma protein;    Retinoblastoma;    Tumor suppressor gene;    E1A protein;    SV40 large T antigen;    RB;    retinoblastoma;    pRB;    retinoblastoma protein;    GST;    glutathione S-transferase;    PMSF;    phenylmethyl-sulfonyl fluoride;    IPTG;    isopropyi β-d-thiogalactopyranoside;   

DOI  :  10.1016/0014-5793(94)80133-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We previously found a new single amino acid substitution at codon 706 (Cys-to-Tyr) of the retinoblastoma (RB) gene in a sporadic retinoblastoma patient. The glutathione S-transferase-RB fused protein containing this mutation was here tested for binding to SV40 large T antigen and adenovirus E1A protein, and was shown to have lost its binding affinity. Thus, Tyr, as well as Phe, residues substituted for Cys⁷⁰⁶ were found to abolish the RB protein activity.

【 授权许可】

Unknown