The Drosophila ninaG Oxidoreductase Acts in Visual Pigment Chromophore Production

Sarfare, Shanta; Ahmad, S. Tariq; Joyce, Michelle V.; Boggess, Bill; O'Tousa, Joseph E.

doi:10.1074/jbc.m412236200

Cited by 35 publications

(37 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Only four of these GMC-like genes have been functionally characterized, all of which are within Drosophila: (i) glucose dehydrogenase, which is regulated by ecdysone and required for eclosion of adult fruit flies and for sperm storage in female D. melanogaster (43,44), (ii) ecdysone oxidase, which is involved in ecdysone metabolism and part of the biosynthesis of unique ecdysteroids (45), and (iii) an oxidoreductase encoded by the ninaG gene and shown to be involved in the production of visual pigment chromophore in Drosophila (46). In A. mellifera, a glucose oxidase has been characterized as being a carbohydrate-metabolizing enzyme involved in the conversion of nectar to honey (47).…”

Section: Discussionmentioning

confidence: 99%

Salicyl Alcohol Oxidase of the Chemical Defense Secretion of Two Chrysomelid Leaf Beetles

Michalski

Mohagheghi

Nimtz

et al. 2008

Journal of Biological Chemistry

View full text Add to dashboard Cite

Salicyl alcohol oxidase is an extracellular enzyme that occurs in glandular reservoirs of chrysomelid leaf beetle larvae and catalyzes the formation of salicylaldehyde, a volatile deterrent used by the larvae against predators. Salicyl alcohol is the hydrolysis product of salicin, a plant-derived precursor taken up by the beetle larvae from the leaves of willow and poplar trees. The cDNA encoding salicyl alcohol oxidase from two related species Chrysomela tremulae and Chrysomela populi has been identified, cloned, and expressed in an active form in Escherichia coli. The open reading frame of 623 amino acids begins in both enzymes with an N-terminal signal peptide of 21 amino acids. Sequence comparison has revealed that salicyl alcohol oxidase belongs to the family of glucose-methanol-choline oxidoreductase-like sequences with mostly unknown function. Enzymes of this family share similar overall structure with an essentially identical FAD-binding site but possess different catalytic activities. The data suggest that salicyl alcohol oxidase, essential for the activation of the plant-derived precursor salicin, was originally recruited from an oxidase involved in the autogenous biosynthesis of iridoid monoterpenes and found in related chrysomelid leaf beetle species.

show abstract

Section: Discussionmentioning

confidence: 99%

Salicyl Alcohol Oxidase of the Chemical Defense Secretion of Two Chrysomelid Leaf Beetles

Michalski

Mohagheghi

Nimtz

et al. 2008

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…The chromophore is transported to the photoreceptor cells where it binds to the opsin resulting in the generation of rhodopsin pigment epithelium (RPE) [72], it appears that Drosophila retinal pigment cells are the closest functional equivalent to the RPE. The ninaG gene encodes an oxidoreductase, which is proposed to act in the conversion of (3R)-3hydroxyretinol to the 3S enantiomer in the compound eye [82,83]. However, it is not known whether ninaG functions in the retinal pigment cells or in photoreceptor cells.…”

Section: Maturation Of Rhodopsinmentioning

confidence: 99%

“…The NINAB BCO subsequently functions in the same neurons and glia as SANTA MARIA in the centric cleavage of β-carotene to retinal [78]. The all-trans-retinol is then transferred to the retinal pigment cells, where it is converted into the chromophore, through a process involving the PINTA retinoid binding protein and the NINAG oxidoreductase [81,82]. This proposed pathway is not yet complete as many factors are still unknown.…”

Section: Maturation Of Rhodopsinmentioning

confidence: 99%

Phototransduction and retinal degeneration in Drosophila

Wang

Montell

2007

Pflugers Arch - Eur J Physiol

261

303

View full text Add to dashboard Cite

Drosophila visual transduction is the fastest known G-protein-coupled signaling cascade and has therefore served as a genetically tractable animal model for characterizing rapid responses to sensory stimulation. Mutations in over 30 genes have been identified, which affect activation, adaptation, or termination of the photoresponse. Based on analyses of these genes, a model for phototransduction has emerged, which involves phosphoinoside signaling and culminates with opening of the TRP and TRPL cation channels. Many of the proteins that function in phototransduction are coupled to the PDZ containing scaffold protein INAD and form a supramolecular signaling complex, the signalplex. Arrestin, TRPL, and Gα q undergo dynamic light-dependent trafficking, and these movements function in long-term adaptation. Other proteins play important roles either in the formation or maturation of rhodopsin, or in regeneration of phosphatidylinositol 4,5-bisphosphate (PIP 2 ), which is required for the photoresponse. Mutation of nearly any gene that functions in the photoresponse results in retinal degeneration. The underlying bases of photoreceptor cell death are diverse and involve mechanisms such as excessive endocytosis of rhodopsin due to stable rhodopsin/arrestin complexes and abnormally low or high levels of Ca 2+ . Drosophila visual transduction appears to have particular relevance to the cascade in the intrinsically photosensitive retinal ganglion cells in mammals, as the photoresponse in these latter cells appears to operate through a remarkably similar mechanism.

show abstract

“…Conversely, ninaG functions in the retina, although the cellular requirement is not known (Sarfare et al, 2005). To address whether pinta functions in pigment or photoreceptor cells, we generated UAS-pinta transgenic flies and crossed the transgenic animals with GAL4 lines, which direct different patterns of expression.…”

Section: Requirement For Pinta In Pigment Cellsmentioning

confidence: 99%

“…Nevertheless, the RBPs and enzymes necessary for conversion of free all-trans-to cis-retinal must exist, because dietary vitamin A is sufficient for production of the 11-cis-retinal. One enzyme that functions in the transformation of the retinal to the chromophore is an oxidoreductase encoded by the neither inactivation nor afterpotential G (ninaG) locus (Sarfare et al, 2005). In addition, two genes (ninaB and ninaD) function outside the retina for production of vitamin A (Stephenson et al, 1983;Gu et al, 2004) and encode a ␤,␤-carotene-15,15Ј-dioxgenase and a class B scavenger receptor, respectively (von Lintig et al, 2001;Kiefer et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Rhodopsin Formation inDrosophilaIs Dependent on the PINTA Retinoid-Binding Protein

Wang¹,

Montell²

2005

J. Neurosci.

View full text Add to dashboard Cite

Retinoids participate in many essential processes including the initial event in photoreception. 11-cis-retinal binds to opsin and undergoes a light-driven isomerization to all-trans-retinal. In mammals, the all-trans-retinal is converted to vitamin A (all-trans-retinol) and is transported to the retinal pigment epithelium (RPE), where along with dietary vitamin A, it is converted into 11-cis-retinal. Although this cycle has been studied extensively in mammals, many questions remain, including the specific roles of retinoid-binding proteins. Here, we establish the Drosophila visual system as a genetic model for characterizing retinoid-binding proteins. In a genetic screen for mutations that affect the biosynthesis of rhodopsin, we identified a novel CRAL-TRIO domain protein, prolonged depolarization afterpotential is not apparent (PINTA), which binds to all-trans-retinol. We demonstrate that PINTA functions subsequent to the production of vitamin A and is expressed and required in the retinal pigment cells. These results represent the first genetic evidence for a role for the retinal pigment cells in the visual response. Moreover, our data implicate Drosophila retinal pigment cells as functioning in the conversion of dietary all-trans-retinol to 11-cis-retinal and suggest that these cells are the closest invertebrate equivalent to the RPE.

show abstract

The Drosophila ninaG Oxidoreductase Acts in Visual Pigment Chromophore Production

Abstract: The Drosophila ninaG mutant is characterized by low levels of Rh1 rhodopsin, because of the inability to transport this rhodopsin from the endoplasmic reticulum to the rhabdomere.

Cited by 35 publications

References 35 publications

Salicyl Alcohol Oxidase of the Chemical Defense Secretion of Two Chrysomelid Leaf Beetles

Salicyl Alcohol Oxidase of the Chemical Defense Secretion of Two Chrysomelid Leaf Beetles

Phototransduction and retinal degeneration in Drosophila

Rhodopsin Formation inDrosophilaIs Dependent on the PINTA Retinoid-Binding Protein

Contact Info

Product

Resources

About