ArticleScientific reports2017
Drosophila melanogaster rhodopsin Rh7 is a UV-to-visible light sensor with an extraordinarily broad absorption spectrum.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 37 citations in OpenAlex.
- A key spectral tuning site of UV-sensitive vertebrate non-visual opsin Opn5.Cellular and molecular life sciences : CMLS · 2025Article
- Development of visible light-sensitive human neuropsin (OPN5) via single amino acid substitution.FEBS letters · 2025Article
- Spectral Tuning in Mammalian Melanopsins.Molecular biology and evolution · 2025Article
- Article
- Control of odor sensation by light and cryptochrome in theiScience · 2025Article
- Adaptive evolution of traits for parasitism and pathogen transmission potential in bat flies.National science review · 2025Article
- Blue and Green Light Responsive Caged Glutamate.Journal of photochemistry and photobiology. A, Chemistry · 2024Article
- Article
- Opsin Gene Duplication in Lepidoptera: Retrotransposition, Sex Linkage, and Gene Expression.Molecular biology and evolution · 2023Article
- Article
- Molecular advances to study the function, evolution and spectral tuning of arthropod visual opsins.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2022Review
- Nocturnal mosquito Cryptochrome 1 mediates greater electrophysiological and behavioral responses to blue light relative to diurnal mosquito Cryptochrome 1.Frontiers in neuroscience · 2022Article
- Weekend Light Shifts Evoke PersistentThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Article
- Unexpected molecular diversity of vertebrate nonvisual opsin Opn5.Biophysical reviews · 2020Review
- Article
- Daytime colour preference in Drosophila depends on the circadian clock and TRP channels.Nature · 2019Article
- Article
- The circadian activity rhythm is reset by nanowatt pulses of ultraviolet light.Proceedings. Biological sciences · 2018Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The genome of Drosophila melanogaster contains seven rhodopsin genes. Rh1-6 proteins are known to have respective absorption spectra and function as visual pigments in ocelli and compound eyes. In contrast, Rh7 protein was recently revealed to function as a circadian photoreceptor in the brain. However, its molecular properties have not been characterized yet. Here we successfully prepared a recombinant protein of Drosophila Rh7 in mammalian cultured cells. Drosophila Rh7 bound both 11-cis-retinal and 11-cis-3-hydroxyretinal to form photo-pigments which can absorb UV light. Irradiation with UV light caused formation of a visible-light absorbing metarhodopsin that activated Gq-type of G protein. This state could be photoconverted back to the original state and, thus Rh7 is a Gq-coupled bistable pigment. Interestingly, Rh7 (lambda max = 350 nm) exhibited an unusual broad spectrum with a longer wavelength tail reaching 500 nm, whose shape is like a composite of spectra of two pigments. In contrast, replacement of lysine at position 90 with glutamic acid caused the formation of a normal-shaped absorption spectrum with maximum at 450 nm. Therefore, Rh7 is a unique photo-sensor that can cover a wide wavelength region by a single pigment to contribute to non-visual photoreception.
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