The Green-absorbing Drosophila Rh6 Visual Pigment Contains a Blue-shifting Amino Acid Substitution That Is Conserved in Vertebrates

Salcedo, Ernesto E.; Farrell, David M.; Zheng, Lijun; Phistry, Meridee; Bagg, Eve E.; Britt, Steven G.

doi:10.1074/jbc.m807368200

Cited by 23 publications

(27 citation statements)

References 47 publications

(53 reference statements)

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“…In addition, this complete wiring diagram of the larval visual system can explain why in previous studies only Rh5-PRs appeared to be required for light avoidance while Rh6-PRs seemed dispensable in most experimental conditions ( Keene et al, 2011 ; Kane et al, 2013 ; Humberg and Sprecher, 2017 ). Moreover, Rh6-PRs mutant larvae were shown to avoid light wavelengths from ultra-violet to green, supporting the idea that Rh5-PRs respond to a wider range of wavelength of light than only ‘blue’ light ( Humberg and Sprecher, 2017 ; Salcedo et al, 2009 ). Taken together, our current data and the lack of evidence of color vision capability in larvae, we propose that the two larval PRs are rather specialized in detection of ambient light intensity and of temporal variations of light intensity.…”

Section: Discussionmentioning

confidence: 53%

Organization of the Drosophila larval visual circuit

Larderet

Fritsch

Gendre

et al. 2017

eLife

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Visual systems transduce, process and transmit light-dependent environmental cues. Computation of visual features depends on photoreceptor neuron types (PR) present, organization of the eye and wiring of the underlying neural circuit. Here, we describe the circuit architecture of the visual system of Drosophila larvae by mapping the synaptic wiring diagram and neurotransmitters. By contacting different targets, the two larval PR-subtypes create two converging pathways potentially underlying the computation of ambient light intensity and temporal light changes already within this first visual processing center. Locally processed visual information then signals via dedicated projection interneurons to higher brain areas including the lateral horn and mushroom body. The stratified structure of the larval optic neuropil (LON) suggests common organizational principles with the adult fly and vertebrate visual systems. The complete synaptic wiring diagram of the LON paves the way to understanding how circuits with reduced numerical complexity control wide ranges of behaviors.

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Section: Discussionmentioning

confidence: 53%

Organization of the Drosophila larval visual circuit

Larderet

Fritsch

Gendre

et al. 2017

eLife

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“…53 Furthermore, A292S mutant yields a blue shift of ~10 to 17 nm in the green-absorbing Drosophila pigment. 54 There are exceptions where, the effect of A292S is negligible and/or gets manifested only in the presence of other mutants. 55 …”

Section: Resultsmentioning

confidence: 99%

Color Vision: “OH-Site” Rule for Seeing Red and Green

et al. 2012

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Eyes gather information and color forms an extremely important component of the information, more so in the case of animals to forage and navigate within their immediate environment. By using the ONIOM (QM/MM) method, we report a comprehensive theoretical analysis of the structure and molecular mechanism of spectral tuning of monkey-red and green-sensitive visual pigments. We show that, interaction of retinal with three hydroxyl-bearing amino acids near the β-ionone ring part of the retinal in opsin, A164S, F261Y and A269T, increases the electron delocalization, decreases the BLA of the retinal and leads to variation in the wavelength of maximal absorbance in the red- and green-sensitive visual pigments. Based on the analysis, we propose the “OH-site” rule for seeing red and green. This rule is also shown to account for the spectral shifts obtained from hydroxyl-bearing amino acids near the Schiff base in different visual pigments: at site 292 (A292S, A292Y, and A292T) in bovine and at site 111 (Y111) in squid opsins. Therefore, the OH-site rule is shown to be site-specific and not pigment-specific and thus can be used for tracking spectral shifts in any visual pigment.

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“…Of particular interest is the serine-to-alanine substitution at the site corresponding to alanine-292 in bovine rhodopsin. In Drosophila, this substitution red-shifts the spectral sensitivity of Rh1 and blueshifts the spectral sensitivity of Rh6 (Salcedo et al, 2009). The presence of a threonine in Ops5 at the site equivalent to the Schiff base counter ion in bovine rhodopsin is particularly unusual (Fig.1).…”

Section: Comparison Between Limulus Ops5 and Limulus Ops1 Andmentioning

confidence: 99%

Opsin co-expression in Limulus photoreceptors: differential regulation by light and a circadian clock

Katti

Kempler

Porter

et al. 2010

Journal of Experimental Biology

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SUMMARYA long-standing concept in vision science has held that a single photoreceptor expresses a single type of opsin, the protein component of visual pigment. However, the number of examples in the literature of photoreceptors from vertebrates and invertebrates that break this rule is increasing. Here, we describe a newly discovered Limulus opsin, Limulus opsin5, which is significantly different from previously characterized Limulus opsins, opsins1 and 2. We show that opsin5 is co-expressed with opsins1 and 2 in Limulus lateral and ventral eye photoreceptors and provide the first evidence that the expression of coexpressed opsins can be differentially regulated. We show that the relative levels of opsin5 and opsin1 and 2 in the rhabdom change with a diurnal rhythm and that their relative levels are also influenced by the animal's central circadian clock. An analysis of the sequence of opsin5 suggests it is sensitive to visible light (400-700nm) but that its spectral properties may be different from that of opsins1 and 2. Changes in the relative levels of these opsins may underlie some of the dramatic day-night changes in Limulus photoreceptor function and may produce a diurnal change in their spectral sensitivity. Supplementary material available online at

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The Green-absorbing Drosophila Rh6 Visual Pigment Contains a Blue-shifting Amino Acid Substitution That Is Conserved in Vertebrates

Cited by 23 publications

References 47 publications

Organization of the Drosophila larval visual circuit

Organization of the Drosophila larval visual circuit

Color Vision: “OH-Site” Rule for Seeing Red and Green

Opsin co-expression in Limulus photoreceptors: differential regulation by light and a circadian clock

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