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(Received for publication, May 6, 1996, and in revised form, June 7, 1996)
§
,
,
,
From the 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.
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
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