Short wavelength-sensitive opsins from the Saharan silver and carpenter Ants

Wc, Smith; Dm, Ayers; Mp, Popp; Pa, Hargrave

doi:10.1007/bf02481714

Cited by 13 publications

(6 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It is possible that Rh7 is a UV-sensitive Rhodopsin, because it retains primary protein sequence motifs that are characteristic of invertebrate UV pigments, such as the lysine at position 168 (position 110 in Rh1) and the DRY motif (Salcedo et al 2003 ; Hu et al 2014 ), but it remains questionable that Rh7 can have λ max below 320 nm. Drosophila UV Rhodopsins, Rh3 and Rh4, have sensitivity maxima at 345 and 375 nm, respectively (Feiler et al 1992 ) and other invertebrate UV Rhodopsins are sensitive in the same wavelength range (Popp et al 1996 ; Smith et al 1997 ; Chase et al 1997 ; Salcedo et al 1999 ). On the other hand, there are also data supporting the notion that Rh7 is sensitive to visible light, because it contains a tyrosine at position 191 that is also present in all other visible-light-detecting Rhodopsins, such as Rh1, Rh2, Rh5, and Rh6, but changed into a phenylalanine in the UV-sensitive Rh3 and Rh4 (Chou et al 1996 ).…”

Section: Discussionmentioning

confidence: 99%

Drosophila Rhodopsin 7 can partially replace the structural role of Rhodopsin 1, but not its physiological function

et al. 2017

View full text Add to dashboard Cite

Rhodopsin 7 (Rh7), a new invertebrate Rhodopsin gene, was discovered in the genome of Drosophila melanogaster in 2000 and thought to encode for a functional Rhodopsin protein. Indeed, Rh7 exhibits most hallmarks of the known Rhodopsins, except for the G-protein-activating QAKK motif in the third cytoplasmic loop that is absent in Rh7. Here, we show that Rh7 can partially substitute Rh1 in the outer receptor cells (R1–6) for rhabdomere maintenance, but that it cannot activate the phototransduction cascade in these cells. This speaks against a role of Rh7 as photopigment in R1–6, but does not exclude that it works in the inner photoreceptor cells.Electronic supplementary materialThe online version of this article (doi:10.1007/s00359-017-1182-8) contains supplementary material, which is available to authorized users.

show abstract

Section: Discussionmentioning

confidence: 99%

Drosophila Rhodopsin 7 can partially replace the structural role of Rhodopsin 1, but not its physiological function

et al. 2017

View full text Add to dashboard Cite

show abstract

“…Squid 1 and 2 are thought to have a max of 494 and 480 nm, respectively (Suzuki et al, 1976;Morris et al, 1993). The desert and carpenter ant UV pigments are thought to have a max of 360 nm, whereas the desert and carpenter ant LW pigments are thought to have a max of 510 nm (Popp et al, 1996;Smith et al, 1997). The bee green pigment is thought to have a max of 526 nm (Chang et al, 1996).…”

Section: Discussionmentioning

confidence: 99%

Blue- and Green-Absorbing Visual Pigments ofDrosophila: Ectopic Expression and Physiological Characterization of the R8 Photoreceptor Cell-Specific Rh5 and Rh6 Rhodopsins

et al. 1999

View full text Add to dashboard Cite

Color discrimination requires the input of different photoreceptor cells that are sensitive to different wavelengths of light. The Drosophila visual system contains multiple classes of photoreceptor cells that differ in anatomical location, synaptic connections, and spectral sensitivity. The Rh5 and Rh6 opsins are expressed in nonoverlapping sets of R8 cells and are the only Drosophila visual pigments that remain uncharacterized. In this study, we ectopically expressed Rh5 and Rh6 in the major class of photoreceptor cells (R1-R6) and show them to be biologically active in their new environment. The expression of either Rh5 or Rh6 in "blind" ninaE(17) mutant flies, which lack the gene encoding the visual pigment of the R1-R6 cells, fully rescues the light response. Electrophysiological analysis showed that the maximal spectral sensitivity of the R1-R6 cells is shifted to 437 or 508 nm when Rh5 or Rh6, respectively, is expressed in these cells. These spectral sensitivities are in excellent agreement with intracellular recordings of the R8p and R8y cells measured in Calliphora and Musca. Spectrophotometric analyses of Rh5 and Rh6 in vivo by microspectrophotometry, and of detergent-extracted pigments in vitro, showed that Rh5 is reversibly photoconverted to a stable metarhodopsin (lambda(max) = 494 nm), whereas Rh6 appears to be photoconverted to a metarhodopsin (lambda(max) = 468 nm) that is less thermally stable. Phylogenetically, Rh5 belongs to a group of short-wavelength-absorbing invertebrate visual pigments, whereas Rh6 is related to a group of long-wavelength-absorbing pigments and is the first member of this class to be functionally characterized.

show abstract

“…Compared to the insect long-wavelength (LW)-sensitive opsin gene family, for which more than 240 complete or partial sequence data are published (Ascher et al, 2001;Briscoe, 2001;Kawakita et al, 2003;Ortiz-Rivas et al, 2004;Spaethe and Briscoe, 2004), only a few UV-sensitive opsin gene sequences are available in GenBank (Briscoe, 2000;Chase et al, 1997;Gao et al, 2000;Kitamoto et al, 2000;Smith et al, 1997;Vanhoutte et al, 2002). We downloaded 13 full-length UV opsin cDNA sequences from four insect orders and the blue-sensitive opsin sequence from Apis mellifera as an outgroup into the Alignment Explorer in MEGA 3.0 (Kumar et al, 2004).…”

Section: Phylogenetic Analysismentioning

confidence: 99%

Molecular characterization and expression of the UV opsin in bumblebees:three ommatidial subtypes in the retina and a new photoreceptor organ in the lamina

Spaethe

Briscoe

2005

Journal of Experimental Biology

103

View full text Add to dashboard Cite

SUMMARY Ultraviolet-sensitive photoreceptors have been shown to be important for a variety of visual tasks performed by bees, such as orientation, color and polarization vision, yet little is known about their spatial distribution in the compound eye or optic lobe. We cloned and sequenced a UV opsin mRNA transcript from Bombus impatiens head-specific cDNA and, using western blot analysis, detected an eye protein band of ∼41 kDa,corresponding to the predicted molecular mass of the encoded opsin. We then characterized UV opsin expression in the retina, ocelli and brain using immunocytochemistry. In the main retina, we found three different ommatidial types with respect to the number of UV opsin-expressing photoreceptor cells,namely ommatidia containing two, one or no UV opsin-immunoreactive cells. We also observed UV opsin expression in the ocelli. These results indicate that the cloned opsin probably encodes the P350 nm pigment, which was previously characterized by physiological recordings. Surprisingly, in addition to expression in the retina and ocelli, we found opsin expression in different parts of the brain. UV opsin immunoreactivity was detected in the proximal rim of the lamina adjacent to the first optic chiasm, which is where studies in other insects have found expression of proteins involved in the circadian clock, period and cryptochrome. We also found UV opsin immunoreactivity in the core region of the antennal lobe glomeruli and different clusters of perikarya within the protocerebrum, indicating a putative function of these brain regions, together with the lamina organ, in the entrainment of circadian rhythms. In order to test for a possible overlap of clock protein and UV opsin spatial expression, we also examined the expression of the period protein in these regions.

show abstract

Short wavelength-sensitive opsins from the Saharan silver and carpenter Ants

Cited by 13 publications

References 30 publications

Drosophila Rhodopsin 7 can partially replace the structural role of Rhodopsin 1, but not its physiological function

Drosophila Rhodopsin 7 can partially replace the structural role of Rhodopsin 1, but not its physiological function

Blue- and Green-Absorbing Visual Pigments ofDrosophila: Ectopic Expression and Physiological Characterization of the R8 Photoreceptor Cell-Specific Rh5 and Rh6 Rhodopsins

Molecular characterization and expression of the UV opsin in bumblebees:three ommatidial subtypes in the retina and a new photoreceptor organ in the lamina

Contact Info

Product

Resources

About