Back to Search Start Over

Light-induced conformational change in rhodopsin detected by modification of G-protein binding, GTP gamma S binding and cGMP phosphodiesterase activation.

Authors :
Pellicone C
Cook NJ
Nullans G
Virmaux N
Source :
FEBS letters [FEBS Lett] 1985 Feb 11; Vol. 181 (1), pp. 184-8.
Publication Year :
1985

Abstract

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, GTP gamma S 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 G alpha 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.

Details

Language :
English
ISSN :
0014-5793
Volume :
181
Issue :
1
Database :
MEDLINE
Journal :
FEBS letters
Publication Type :
Academic Journal
Accession number :
2982652
Full Text :
https://doi.org/10.1016/0014-5793(85)81139-x