Light‐induced conformational change in rhodopsin detected by modification of G‐protein binding, GTPγS binding and cGMP phosphodiesterase activation

FEBS Letters

Virmaux, N.¹  Pellicone, C.¹  Nullans, G.¹  Cook, N.J.¹ 

[1] Centre de Neurochimie, 5, Rue Blaise Pascal, 67084 Strasbourg Cédex, France

关键词: Rhodopsin;    G-protein;    GTP binding;    cGMP phosphodiesterase;    CNBr digestion;    Conformational change;    G-protein;    GTP binding protein or transducin;    PDE;    phosphodiesterase;    ROS;    rod outer segments;    GTPγS;    non-hydrolyzable GTP 35S γ-labeled;    ROS;    rod outer segments;   

DOI  :  10.1016/0014-5793(85)81139-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

CNBr treatment of rod outer segments was performed in dark and in light conditions. With the subsequent modified rhodopsin and opsin the cGMP phosphodiesterase activation system was reconstituted. The recombination systems exhibited greatly reduced G-protein binding, GTPγS binding and cGMP phosphodiesterase activation. The reduction in activity of these three steps of the PDE activation cascade is most significant with modified opsin and is shown to be due to its inability to bind the Gα subunit. The correlation between the localization of CNBr cleavage in dark and light conditions and these results is strongly indicative that a light-induced conformational change occurs in two extradiscal regions of rhodopsin.

【 授权许可】

Unknown