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The effect of proteolytic removal of the C-terminal fragment of rhodopsin on its ability to activate visual cascade. Vliianie proteoliticheskogo otshchepleniia C-kontsevogo fragmenta rodopsina na ego sposobnost' aktivirovat' zritel'nyi kaskadстатья
- Авторы: Komolov K.E., Senin I.I., Filippov P.
- Журнал: Bioorganicheskaia khimiia
- Том: 28
- Номер: 1
- Год издания: 2002
- Первая страница: 16
- Последняя страница: 22
- Аннотация: The role of the C-terminal domain of rhodopsin in the activation of transducin was studied. The treatment of photoreceptor membranes with trypsin, thermolysin, and Asp-N-endoprotease led to the respective rhodopsin species devoid of 9, 12-, or 19-aa C-terminal fragments. It was shown that the removal of 9-aa fragment by trypsin does not affect the catalytic activity of the receptor, whereas the thermolysin-induced truncation of the rhodopsin C-terminus by 12 aa about 1.5-fold enhances its activity. The Asp-N-endoprotease-assisted removal of 19 aa (i.e., the shortening by seven more C-terminal aa) virtually unchanges the rhodopsin catalytic activity compared to the preparation truncated with thermolysin. These results suggest that the part of the rhodopsin C-terminal fragment between the sites of its cleavage by trypsin and thermolysin (Val337-Ser338-Lys339) inhibits the signal transduction from rhodopsin to the next component of visual cascade.
- Добавил в систему: Сенин Иван Иванович