Sulfhydryl group modification of photoreceptor G‐protein prevents its light‐induced binding to rhodopsin

FEBS Letters

Reichert, J.¹  Hofmann, K.P.¹ 

[1] Institut für Biophysik und Strahlenbiologie, Universität Freiburg im Breisgau, Albertstr. 23, D-7800 Freiburg, FRG

关键词: Sulfhydryl modification;    Photoreceptor;    Peripheral membrane protein;    GTP-binding protein;    Rhodopsin;    Protein-protein interaction;    ROS;    rod outer segments;    G;    G-protein or GTP-binding protein or transducin;    NIR;    near infrared;    R*;    photoexcited rhodopsin;    GTP-γS;    guanosine 5′-O-(3-thiotriphosphate);    DTNB;    5;    5′-dithiobis(2-nitrobenzoic acid);    NEM;    N-ethylmaleimide;    2-PDS;    2;    2′-dithiodipyridine;    DTT;    dithiothreitol;    Pipes;    piperazine-1;    4-diethanesulfonic acid;   

DOI  :  10.1016/0014-5793(84)80219-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The effect of sulfhydryl modification on the light-induced interaction between rhodopsin and the peripheral GTP-binding protein of the photoreceptor membrane (G-protein) has been investigated by time-resolved near-infrared light-scattering and polyacrylamide gel electrophoresis. It has been found that the modification of rhodopsin with the alkylating agent N-ethylmaleimide (NEM) does not affect its light-induced interaction with the G-protein. Modification of G-protein with NEM or other sulfhydryl agents prevents any light-induced binding to rhodopsin. Dark-associatiion of G to the membrane as well as the light-induced complex with rhodopsin (once formed) is insensitive to NEM.

【 授权许可】

Unknown