cDNA, from Hevea brasiliensis latex, encoding 1-deoxy-d-xylulose-5-phosphate reductoisomerase

Yoonram, Krueawan; Takahashi, Shigetoshi; Rattanapittayaporn, Atiya; Koyama, Tanetoshi; Wititsuwannakul, Dhirayos; Wititsuwannakul, Rapepun

doi:10.1016/j.plantsci.2008.07.005

Cited by 5 publications

(1 citation statement)

References 33 publications

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“…3). Therefore, SmDXR was considered to be a constitutively expressing gene, which is similar with the most DXRs such as Camptotheca acuminata (Yao et al 2008), Rauvolfia verticillata (Liao et al 2007), Ginkgo biloba (Gong et al 2005) and Hevea brasiliensis (Yoonram et al 2008). This is the first report on the mRNA expression profile of genes encoding key enzymes involved in tanshinones biosynthetic pathway in different tissues of S. miltiorrhiza plants.…”

Section: Tissue Expression Analysis Of Smdxrmentioning

confidence: 99%

Molecular characterization and expression of 1-deoxy-d-xylulose 5-phosphate reductoisomerase (DXR) gene from Salvia miltiorrhiza

et al. 2009

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Section: Tissue Expression Analysis Of Smdxrmentioning

confidence: 99%

Molecular characterization and expression of 1-deoxy-d-xylulose 5-phosphate reductoisomerase (DXR) gene from Salvia miltiorrhiza

et al. 2009

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Optimization of the transient transformation of Catharanthus roseus cells by particle bombardment and its application to the subcellular localization of hydroxymethylbutenyl 4-diphosphate synthase and geraniol 10-hydroxylase

et al. 2009

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The monoterpene indole alkaloids (MIA) synthesized in Catharanthus roseus are highly valuable metabolites due to their pharmacological properties. In planta, the MIA biosynthetic pathway exhibits a complex compartmentation at the cellular level, whereas subcellular data are sparse. To gain insight into this level of organization, we have developed a high efficiency green fluorescent protein (GFP) imaging approach to systematically localize MIA biosynthetic enzymes within C. roseus cells following a biolistic-mediated transient transformation. The biolistic transformation protocol has been first optimized to obtain a high number of transiently transformed cells with a ~12-fold increase compared to previous protocols and thus to clearly and easily identify the fusion GFP expression patterns in numerous cells. On the basis of this protocol, the subcellular localization of hydroxymethylbutenyl 4-diphosphate synthase (HDS), a methyl erythritol phosphate pathway enzyme and geraniol 10-hydroxylase (G10H), a monoterpene-secoiridoid pathway enzyme has been next characterized. Besides showing the accumulation of HDS within plastids of C. roseus cells, we also provide evidences of the presence of HDS in long stroma-filled thylakoid-free extensions budding from plastids, i.e. stromules that are in close association with other organelles such as endoplasmic reticulum (ER) or mitochondria in agreement with their proposed function in enhancing interorganelle metabolite exchanges. Furthermore, we also demonstrated that G10H is an ER-anchored protein, consistent with the presence of a transmembrane helix at the G10H N-terminal end, which is both necessary and sufficient to drive the ER anchoring.

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Flowery odor formation revealed by differential expression of monoterpene biosynthetic genes and monoterpene accumulation in rose (Rosa rugosa Thunb.)

Liu

Chen

et al. 2014

Plant Physiology and Biochemistry

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cDNA, from Hevea brasiliensis latex, encoding 1-deoxy-d-xylulose-5-phosphate reductoisomerase

Cited by 5 publications

References 33 publications

Molecular characterization and expression of 1-deoxy-d-xylulose 5-phosphate reductoisomerase (DXR) gene from Salvia miltiorrhiza

Molecular characterization and expression of 1-deoxy-d-xylulose 5-phosphate reductoisomerase (DXR) gene from Salvia miltiorrhiza

Optimization of the transient transformation of Catharanthus roseus cells by particle bombardment and its application to the subcellular localization of hydroxymethylbutenyl 4-diphosphate synthase and geraniol 10-hydroxylase

Flowery odor formation revealed by differential expression of monoterpene biosynthetic genes and monoterpene accumulation in rose (Rosa rugosa Thunb.)

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