| Literature DB >> 12565839 |
Takeshi Suzuki1, Kenta Yamasaki, Satoshi Fujita, Kazushi Oda, Mineo Iseki, Kazuichi Yoshida, Masakatsu Watanabe, Hiromi Daiyasu, Hiroyuki Toh, Eriko Asamizu, Satoshi Tabata, Kenji Miura, Hideya Fukuzawa, Shogo Nakamura, Tetsuo Takahashi.
Abstract
Phototaxis in the unicellular green alga Chlamydomonas reinhardtii is mediated by rhodopsin-type photoreceptor(s). Recent expressed sequence tag database from the Kazusa DNA Research Institute has provided the basis for unequivocal identification of two archaeal-type rhodopsins in it. Here we demonstrate that one is located near the eyespot, wherein the photoreceptor(s) has long been thought to be enriched, along with the results of bioinformatic analyses. Secondary structure prediction showed that the second putative transmembrane helices (helix B) of these rhodopsins are rich in glutamate residues, and homology modeling suggested that some additional intra- or intermolecular interactions are necessary for opsin-like folding of the N-terminal ca. 300-aa membrane spanning domains of 712 and 737-aa polypeptides. These results complement physiological and electrophysiological experiments combined with the manipulation of their expression [O.A. Sineshchekov, K.H. Jung, J.H. Spudich, Proc. Natl. Sci. USA 99 (2002) 8689; G. Nagel, D. Olig, M. Fuhrmann, S. Kateriya, A.M. Musti, E. Bamberg, P. Hegemann, Science 296 (2002) 2395].Entities:
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Year: 2003 PMID: 12565839 DOI: 10.1016/s0006-291x(02)03079-6
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575