Evidence for the archaebacterial‐type conformation about the bond between the β‐ionone ring and the polyene chain of the chromophore retinal in chlamyrhodopsin

FEBS Letters

Takahashi, Tetsuo²  Goshima, Takehiko²  Wada, Akimori¹  Ito, Masayoshi¹  Akai, Akiko¹  Sakamoto, Masaru² 

[1] Kobe Pharmaceutical University, Higashinada, Kobe 658-8558, Japan;School of Materials Science, Japan Advanced Institute of Science and Technology, Tatsunokuchi, Ishikawa 923-1292, Japan

关键词: Retinal analog;    Phoborhodopsin;    Bacteriorhodopsin;    Phototaxis;    Chlamydomonas reinhardtii;    Halobacterium salinarum;   

DOI  :  10.1016/S0014-5793(98)01004-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Previous studies using retinal analogs (Wada, A., Sakai, M., Kinumi, T., Tsujimoto, K., Yamauchi, M. and Ito, M. (1994) J. Org. Chem. 59, 6992–6997; Wada, A., Sakai, M., Imamoto, Y., Shichida., Y., Yoshizawa, T. and Ito, M. (1993) Chem. Pharm. Bull. 41, 793–795) revealed that both retinochrome and visual pigments share a common chromophoric conformation in which the ring region of retinal is twisted ca. 50° with respect to the plane of the polyene chain, suggesting a highly conserved 6-s-cis conformation throughout rhodopsin-like pigments in animals. By contrast, 6-s-trans conformation was commonly observed or suggested in archaebacterial rhodopsins examined thus far. Here we have reconstituted in vivo both the photoreceptor for photobehavioral responses of the unicellular alga Chlamydomonas reinhardtii and the second archaeal sensory photoreceptor phoborhodopsin from a series of retinal analogs. Results exclusively point to the conclusion that in both photoreceptors retinal has the coplanar 6-s-trans conformation, though recent molecular cloning studies revealed no homology between Chlamydomonas photoreceptor (chlamyrhodopsin) and archaeal rhodopsins.

【 授权许可】

Unknown