期刊
COMMUNICATIONS BIOLOGY
卷 2, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s42003-019-0409-3
关键词
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资金
- JSPS KAKENHI [15H05777, 26291070, 16KT0074, 17H06015]
- JST CREST [JPMJCR1753]
- Human Frontier Science Program [RGP0034/2014]
- Swiss National Science Foundation [173335, 160805]
- European Community [290605]
- Swiss National Supercomputing Centre
- Grants-in-Aid for Scientific Research [16KT0074, 26291070, 17H06015] Funding Source: KAKEN
Animals sense light using photosensitive proteins-rhodopsins-containing a chromophore-retinal-that intrinsically absorbs in the ultraviolet. Visible light-sensitivity depends primarily on protonation of the retinylidene Schiff base (SB), which requires a negatively-charged amino acid residue-counterion-for stabilization. Little is known about how the most common counterion among varied rhodopsins, Glu181, functions. Here, we demonstrate that in a spider visual rhodopsin, orthologue of mammal melanopsins relevant to circadian rhythms, the Glu181 counterion functions likely by forming a hydrogen-bonding network, where Ser186 is a key mediator of the Glu181-SB interaction. We also suggest that upon light activation, the Glu181-SB interaction rearranges while Ser186 changes its contribution. This is in contrast to how the counterion of vertebrate visual rhodopsins, Glu113, functions, which forms a salt bridge with the SB. Our results shed light on the molecular mechanisms of visible light-sensitivity relevant to invertebrate vision and vertebrate non-visual photoreception.
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