Molecular Cloning and Characterization of a Trichome-Specific Promoter of Artemisinic Aldehyde Δ11(13) Reductase (DBR2) in Artemisia annua

Jiang, Weimin; Lu, Xu; Qiu, Bo; Zhang, Fangyuan; Shen, Qian; Lv, Zongyou; Fu, Xueqing; Yan, Tingxiang; Gao, Erdi; Zhu, Mengmeng; Chen, Lingxian; Zhang, Ling; Wang, Guofeng; Sun, Xiaofen; Tang, Kexuan

doi:10.1007/s11105-013-0603-2

Cited by 30 publications

(19 citation statements)

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“…Among the four genes, only ADS , CYP71AV1 and DBR2 have W‐box motifs in their promoters (Fig. S2a; Wang et al ., , , ; Jiang et al ., ; Yang et al ., ). The yeast one‐hybrid assay showed that AaGSW1 only bound to one of the W‐box motifs in the promoter of CYP71AV1 (pCYP71AV1), while AaWRKY75b bound to none of them (Figs a, S2b).…”

Section: Resultsmentioning

confidence: 99%

“…Artemisinin is biosynthesized in A. annua via a glandular trichome-specific metabolic pathway (Olofsson et al, 2012). The four key genes ADS, CYP71AV1, DBR2 and ALDH1 of the artemisinin biosynthetic pathway were identified to have the trichome-specific expression patterns as reported by the promoter-GUS fusion assays (Wang et al, , 2012(Wang et al, , 2016Jiang et al, 2014). Although a few transcription factors that regulate artemisinin biosynthesis have been identified, knowledge about how this regulatory network functions is far from complete (Shen et al, 2016b).…”

Section: Discussionmentioning

confidence: 99%

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GLANDULAR TRICHOME‐SPECIFIC WRKY 1 promotes artemisinin biosynthesis in Artemisia annua

et al. 2016

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Artemisinin is a type of sesquiterpene lactone well known as an antimalarial drug, and is specifically produced in glandular trichomes of Artemisia annua. However, the regulatory network for the artemisinin biosynthetic pathway remains poorly understood. Exploration of trichome-specific transcription factors would facilitate the elucidation of regulatory mechanism of artemisinin biosynthesis. The WRKY transcription factor GLANDULAR TRICHOME-SPECIFIC WRKY 1 (AaGSW1) was cloned and analysed in A. annua. AaGSW1 exhibited similar expression patterns to the trichome-specific genes of the artemisinin biosynthetic pathway and AP2/ERF transcription factor AaORA. A β-glucuronidase (GUS) staining assay further demonstrated that AaGSW1 is a glandular trichome-specific transcription factor. AaGSW1 positively regulates CYP71AV1 and AaORA expression by directly binding to the W-box motifs in their promoters. Overexpression of AaGSW1 in A. annua significantly improves artemisinin and dihydroartemisinic acid contents; moreover, AaGSW1 can be directly regulated by AaMYC2 and AabZIP1, which are positive regulators of jasmonate (JA)- and abscisic acid (ABA)-mediated artemisinin biosynthetic pathways, respectively. These results demonstrate that AaGSW1 is a glandular trichome-specific WRKY transcription factor and a positive regulator in the artemisinin biosynthetic pathway. Moreover, we propose that two trifurcate feed-forward pathways involving AaGSW1, CYP71AV1 and AaMYC2/AabZIP1 function in the JA/ABA response in A. annua.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

GLANDULAR TRICHOME‐SPECIFIC WRKY 1 promotes artemisinin biosynthesis in Artemisia annua

et al. 2016

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“…4b). In the CYP71AV1 promoter (FJ870128; Wang et al, 2012), the two boxes are a long way apart, whereas in the DBR2 promoter (KC347592 and KC347593, Jiang et al, 2014), they are close to each other (Fig. 4b).…”

Section: Researchmentioning

confidence: 96%

The jasmonate‐responsive AaMYC2 transcription factor positively regulates artemisinin biosynthesis in Artemisia annua

et al. 2016

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SummaryThe plant Artemisia annua is well known due to the production of artemisinin, a sesquiterpene lactone that is widely used in malaria treatment. Phytohormones play important roles in plant secondary metabolism, such as jasmonic acid (JA), which can induce artemisinin biosynthesis in A. annua. Nevertheless, the JA-inducing mechanism remains poorly understood.The expression of gene AaMYC2 was rapidly induced by JA and AaMYC2 binds the G-boxlike motifs within the promoters of gene CYP71AV1 and DBR2, which are key structural genes in the artemisinin biosynthetic pathway.Overexpression of AaMYC2 in A. annua significantly activated the transcript levels of CYP71AV1 and DBR2, which resulted in an increased artemisinin content. By contrast, artemisinin content was reduced in the RNAi transgenic A. annua plants in which the expression of AaMYC2 was suppressed. Meanwhile, the RNAi transgenic A. annua plants showed lower sensitivity to methyl jasmonate treatment than the wild-type plants.These results demonstrate that AaMYC2 is a positive regulator of artemisinin biosynthesis and is of great value in genetic engineering of A. annua for increased artemisinin production.

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“…The artemisinin biosynthetic pathway has been studied for many years, and most of the enzymes have already been cloned [37–39]. In the artemisinin biosynthesis, artemisinic aldehyde Δ11(13) reductase (DBR) can convert artemisinic aldehyde into dihydroartemisinic aldehyde [30].…”

Section: Discussionmentioning

confidence: 99%

Cloning and characterization of enoate reductase with high β-ionone to dihydro-β-ionone bioconversion productivity

et al. 2018

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BackgroundDihydro-β-ionone is a principal aroma compound and has received considerable attention by flavor and fragrance industry. The traditional method of preparing dihydro-β-ionone has many drawbacks, which has restricted its industrial application. Therefore, it is necessary to find a biotechnological method to produce dihydro-β-ionone.ResultsIn this study, the enoate reductase with high conversion efficiency of β-ionone to dihydro-β-ionone, DBR1, was obtained by screening four genetically engineered bacteria. The product, dihydro-β-ionone, was analyzed by GC and GC-MS. The highest dihydro-β-ionone production with 308.3 mg/L was detected in the recombinant strain expressing DBR1 which was later on expressed and purified. Its optimal temperature and pH were 45 °C and 6.5, respectively. The greatest activity of the purified enzyme was 356.39 U/mg using β-ionone as substrate. In the enzymatic conversion system, 1 mM of β-ionone was transformed into 91.08 mg/L of dihydro-β-ionone with 93.80% of molar conversion.ConclusionDBR1 had high selectivity to hydrogenated the 10,11-unsaturated double bond of β-ionone as well as high catalytic efficiency for the conversion of β-ionone to dihydro-β-ionone. It is the first report on the bioconversion of β-ionone to dihydro-β-ionone by using enoate reductase.Electronic supplementary materialThe online version of this article (10.1186/s12896-018-0438-x) contains supplementary material, which is available to authorized users.

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Molecular Cloning and Characterization of a Trichome-Specific Promoter of Artemisinic Aldehyde Δ11(13) Reductase (DBR2) in Artemisia annua

Cited by 30 publications

References 52 publications

GLANDULAR TRICHOME‐SPECIFIC WRKY 1 promotes artemisinin biosynthesis in Artemisia annua

GLANDULAR TRICHOME‐SPECIFIC WRKY 1 promotes artemisinin biosynthesis in Artemisia annua

The jasmonate‐responsive AaMYC2 transcription factor positively regulates artemisinin biosynthesis in Artemisia annua

Cloning and characterization of enoate reductase with high β-ionone to dihydro-β-ionone bioconversion productivity

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