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Volume 271, Number 35, Issue of August 30, 1996 pp. 21359-21364
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Photoreceptor Protein s26, a Cone Homologue of S-modulin in Frog Retina

(Received for publication, May 6, 1996, and in revised form, June 7, 1996)

Satoru Kawamura Dagger § , Osamu Kuwata Dagger , Motoyuki Yamada Dagger , Shinji Matsuda '' , Osamu Hisatomi '' and Fumio Tokunaga ''

From the Dagger  Department of Physiology, Keio University School of Medicine, Shinano-machi 35, Shinjuku-ku, Tokyo 160, and the Departments of § Biology and '' Earth and Space Science, Graduate School of Science, Osaka University, Machikane-yama 1-1, Toyonaka, Osaka 560, Japan

A frog retinal protein named s26 is a 26-kDa protein found during purification of S-modulin in frog retina (Kawamura, S. (1992) Photochem. Photobiol. 56, 1173-1180). To identify its role in frog retina, first s26 was purified to nearly homogeneity with three chromatographical steps. Based on the partial amino acid sequences of the proteolysed fragments of s26, we isolated cDNAs that encode s26. The analysis of its amino acid sequence revealed that s26 is an S-modulin-like protein, while it shows higher homology to visinin. Visinin is a Ca2+-binding protein reported to be present in chicken cones, but its localization in the retina had been a subject in dispute. The present study showed that s26 is present in cone photoreceptors. The study also showed that s26 inhibits phosphorylation of rhodopsin after a light flash at high Ca2+ concentrations as S-modulin does. From these results, we concluded that s26 is a cone homologue of S-modulin. The result is consistent with the idea that each type of photoreceptors expresses each cell-type specific version of phototransduction proteins.


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