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. 2014 Mar 12;9(3):e91323. doi: 10.1371/journal.pone.0091323

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© 2014 Sasaki et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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G-protein activation by PR/Rh chimera (a), bovine Rh (b), and GR/Rh chimeras (c). Time-dependent GTPγS-binding to transducin was monitored under light (open circle or square) and dark (filled circle or square) conditions. Solid lines in (a) represent the results of PR/Rh225-252, while dotted lines in (a) represent WT PR. Solid lines in (b, c) represent the results of GR/Rh225-252 and GR/Rh225-252 + E132Q, while dotted lines in (b) and (c) represent bovine Rh and GR/Rh225-252, respectively. The concentrations of bovine Rh, PR (PR chimera) and GR (GR chimera) are 5 nM, 2.1 μM, and 1.9 μM, respectively. Binding at t = 0 was caused by unspecific binding to the filter and was not used to assay the catalytic activities of pigments. (d) Comparison of G-protein activation ability by PR/Rh and GR/Rh chimeras. GTPγS-binding to transducin was monitored at 10 min under light (open bar) and dark (filled bar) conditions. Data are presented as the means ± S.D. of more than three independent experiments.