Characterization of the novel role of NinaB orthologs from Bombyx mori and Tribolium castaneum

Chai, Chun-Li; Xu, Xin; Sun, Weizhong; Zhang, Fang; Ye, Chuan; Ding, Guangshu; Li, Jiantao; Zhong, Guoxuan; Xiao, Wei; Liu, Binbin; Lintig, Johannes von; Lü, Cheng

doi:10.1016/j.ibmb.2019.03.004

Cited by 7 publications

(4 citation statements)

References 44 publications

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“…Similarly, to produce the vertebrate visual chromophore (11-cis-retinal), RPE65 cleaves the O-alkyl ester bond of all-trans-retinyl ester and then isomerizes the retinyl moiety to produce 11-cisretinol [26,27] that is subsequently oxidized to 11-cis-retinal by retinol dehydrogenase 5. It has been proposed that only one-half of the carotenoid substrate is isomerized by the moth Galleria NinaB enzyme (gNinaB) [29], and, recently, this has been reported for several other insect species [30]. Therefore, both enzymes are able to isomerize a conjugated C20 fragment from all-trans to the 11-cis configuration.…”

Section: Carotenoid Cleavage Oxygenase Superfamily and Their Versatilitymentioning

confidence: 99%

“…The mechanism of isomerization by RPE65, on the one hand, had been controversial [25,26] but more recent structural studies with inhibitors [33,34] and using site-directed mutagenesis [27,65] point to the formation of a delocalized carbocation and the transient destabilization of the double bond order upon O-alkyl cleavage as prerequisite to isomerization. For gNinaB, on the other hand, it is possible the all-trans to 11-cis isomerization could be driven by the oxidative cleavage of the carotenoid, though this is much less well established [29,30].…”

Section: Carotenoid Cleavage Oxygenase Superfamily and Their Versatilitymentioning

confidence: 99%

See 1 more Smart Citation

Evolutionary aspects and enzymology of metazoan carotenoid cleavage oxygenases

Poliakov

Uppal

Rogozin

et al. 2020

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

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Section: Carotenoid Cleavage Oxygenase Superfamily and Their Versatilitymentioning

confidence: 99%

Section: Carotenoid Cleavage Oxygenase Superfamily and Their Versatilitymentioning

confidence: 99%

Evolutionary aspects and enzymology of metazoan carotenoid cleavage oxygenases

Poliakov

Uppal

Rogozin

et al. 2020

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

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“…NinaB is required by Drosophila for vision and can metabolize carotenoids into visual chromophores [14]. In addition, Chai et al (2019) discovered that NinaB is involved in the reproduction of the silkworm Bombyx mori and the flour beetle Tribolium castaneum [15]. Furthermore, a gene named Carotenoid Oxygenases and Retinal Isomerase (BmCORI) has been identified in B. mori; this may play a pivotal role in the β-carotene metabolism [16].…”

Section: Of 15mentioning

confidence: 99%

NinaB and BCO Collaboratively Participate in the β-Carotene Catabolism in Crustaceans: A Case Study on Chinese Mitten Crab Eriocheir sinensis

Zhang,

Xiong,

Yang

et al. 2024

IJMS

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Carotenoid cleavage oxygenases can cleave carotenoids into a range of biologically important products. Carotenoid isomerooxygenase (NinaB) and β, β-carotene 15, 15′-monooxygenase (BCO1) are two important oxygenases. In order to understand the roles that both oxygenases exert in crustaceans, we first investigated NinaB-like (EsNinaBl) and BCO1-like (EsBCO1l) within the genome of Chinese mitten crab (Eriocheir sinensis). Their functions were then deciphered through an analysis of their expression patterns, an in vitro β-carotene degradation assay, and RNA interference. The results showed that both EsNinaBl and EsBCO1l contain an RPE65 domain and exhibit high levels of expression in the hepatopancreas. During the molting stage, EsNinaBl exhibited significant upregulation in stage C, whereas EsBCO1l showed significantly higher expression levels at stage AB. Moreover, dietary supplementation with β-carotene resulted in a notable increase in the expression of EsNinaBl and EsBCO1l in the hepatopancreas. Further functional assays showed that the EsNinaBl expressed in E. coli underwent significant changes in its color, from orange to light; in addition, its β-carotene cleavage was higher than that of EsBCO1l. After the knockdown of EsNinaBl or EsBCO1l in juvenile E. sinensis, the expression levels of both genes were significantly decreased in the hepatopancreas, accompanied by a notable increase in the redness (a*) values. Furthermore, a significant increase in the β-carotene content was observed in the hepatopancreas when EsNinaBl-mRNA was suppressed, which suggests that EsNinaBl plays an important role in carotenoid cleavage, specifically β-carotene. In conclusion, our findings suggest that EsNinaBl and EsBCO1l may exhibit functional co-expression and play a crucial role in carotenoid cleavage in crabs.

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“…Carotenoids are involved in blocking ultraviolet light and directly quenching singlet oxygen to prevent free radicals from damaging cells (Carroll & Berenbaum, 2006; Toews et al ., 2017) and in regulating body color changes (Chai et al ., 2019; Yang et al ., 2019). Carotenoids also affect insect behavior, including visual sensitivity and phototactic responses (Shimizu et al ., 1976; Stark & Zitzmann, 1976; Lintig et al ., 2001), mating behavior (Andersson et al ., 2007), reproductive capacity (Chai et al ., 2019), and diapause ability (Veerman, 2001; Bryon et al ., 2017).…”

Section: Introductionmentioning

confidence: 99%

Characterization of carotenoid biosynthetic pathway genes in the pea aphid (Acyrthosiphon pisum) revealed by heterologous complementation and RNA interference assays

et al. 2021

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Carotenoids are involved in many essential physiological functions and are produced from geranylgeranyl pyrophosphate through synthase, desaturase, and cyclase activities. In the pea aphid (Acyrthosiphon pisum), the duplication of carotenoid biosynthetic genes, including carotenoid synthases/cyclases (ApCscA–C) and desaturases (ApCdeA–D), through horizontal gene transfer from fungi has been detected, and ApCdeB has known dehydrogenation functions. However, whether other genes contribute to aphid carotenoid biosynthesis, and its specific regulatory pathway, remains unclear. In the current study, functional analyses of seven genes were performed using heterologous complementation and RNA interference assays. The bifunctional enzymes ApCscA–C were responsible for the synthase of phytoene, and ApCscC may also have a cyclase activity. ApCdeA, ApCdeC, and ApCdeD had diverse dehydrogenation functions. ApCdeA catalyzed the enzymatic conversion of phytoene to neurosporene (three‐step product), ApCdeC catalyzed the enzymatic conversion of phytoene to ζ‐carotene (two‐step product), and ApCdeD catalyzed the enzymatic conversion of phytoene to lycopene (four‐step product). Silencing of ApCscs reduced the expression levels of ApCdes, and silencing these carotenoid biosynthetic genes reduced the α‐, β‐, and γ‐carotene levels, as well as the total carotenoid level. The results suggest that these genes were activated and led to carotenoid biosynthesis in the pea aphid.

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Characterization of the novel role of NinaB orthologs from Bombyx mori and Tribolium castaneum

Cited by 7 publications

References 44 publications

Evolutionary aspects and enzymology of metazoan carotenoid cleavage oxygenases

Evolutionary aspects and enzymology of metazoan carotenoid cleavage oxygenases

NinaB and BCO Collaboratively Participate in the β-Carotene Catabolism in Crustaceans: A Case Study on Chinese Mitten Crab Eriocheir sinensis

Characterization of carotenoid biosynthetic pathway genes in the pea aphid (Acyrthosiphon pisum) revealed by heterologous complementation and RNA interference assays

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