Evidence for the archaebacterial-type conformation about the bond between the beta-ionone ring and the polyene chain of the chromophore retinal in chlamyrhodopsin.

Abstract:

: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 degrees 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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Sakamoto M,Wada A,Akai A,Ito M,Goshima T,Takahashi T

doi

10.1016/s0014-5793(98)01004-7

subject

Has Abstract

pub_date

1998-09-04 00:00:00

pages

335-8

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(98)01004-7

journal_volume

434

pub_type

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