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Fig. 5 | Zoological Letters

Fig. 5

From: Spectral tuning mediated by helix III in butterfly long wavelength-sensitive visual opsins revealed by heterologous action spectroscopy

Fig. 5

Contribution of single mutations in helix III for the red-shift in a chimera Rh3(I)/Rh1(II-VII). The absorption spectra of chimeric mutants Rh3(I)/Rh1(II-VII) having a single mutation at positions in which amino acid residues are different between PxRh1 and PxRh3in helix III (a, highlighted with grey boxes), Rh3(I)/Rh1(II-VII)_A109F (b), Rh3(I)/Rh1(II-VII)_L112I (c), Rh3(I)/Rh1(II-VII)_A115C (d), Rh3(I)/Rh1(II-VII)_A115G (e), Rh3(I)/Rh1(II-VII)_F120Y (f), Rh3(I)/Rh1(II-VII)_I123V (g), Rh3(I)/Rh1(II-VII)_M130A (h) estimated by heterologous action spectroscopy. Solid circles represent the mean relative sensitivities of cultured cells expressing each chimeric mutant at each wavelength of light irradiation (n = 3) and black curves indicate estimated absorption spectra. The error bar shows standard error. The absorption spectra of PxRh1_Gs and PxRh3_Gs are also indicated by green and magenta broken curves, respectively. Schematic drawings of seven transmembrane structures of butterfly opsins are also shown, in which helices and amino acid residues of PxRh1 and PxRh3 are indicated by green and magenta, respectively

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Zoological Letters

ISSN: 2056-306X

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