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Sulfhydryl group modification of photoreceptor G‐protein prevents its light‐induced binding to rhodopsin
Author(s) -
Reichert J.,
Hofmann K.P.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80219-7
Subject(s) - rhodopsin , chemistry , posttranslational modification , biophysics , microbiology and biotechnology , biochemistry , biology , retinal , enzyme
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.