ArticlePlanta2026
Functional and biosynthetic investigation of polyisoprenoids in roses leaves.
Article in Planta, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
- From Isoprene Units to Polyprenols and Dolichols: 70 Years of Polyisoprenoid Biosynthesis Research.Cell biochemistry and biophysics · 2026Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
MAIN
conclusionIn Rosa chinensis, four distinct polyisoprenoid families, including two very long-chain types, are synthesized by only three cis-prenyltransferases, challenging the traditional one-enzyme-one-family model. The presence of very long polyisoprenoids in leaves and young shoots is most probably involved in plant organ development. Although terpenoids in roses have been extensively studied, the polyisoprenoid fraction has remained unexplored. In this work, we provide the first characterization of polyisoprenoid diversity and biosynthesis in roses, revealing unexpected chemical and enzymatic complexity. Four distinct polyisoprenoid families (7-9, 15-25, 26-34, and 35-50 isoprene units) were identified in Rosa chinensis, with very long-chain compounds accumulated in leaves and young shoots. We functionally characterized three cis-prenyltransferases (CPTs) and a CPT-binding partner, RcNUS1, involved in their biosynthesis. The chloroplast-localized RcCPT2 synthesizes short-chain polyisoprenoids, whereas two endoplasmic reticulum-localized heteromeric enzymes, RcCPT1 and RcCPT3, require RcNUS1 as a partner to produce longer-chain compounds. Phylogenetic analysis revealed strong evolutionary conservation but notable species-specific diversification of these enzymes. Remarkably, the number of polyisoprenoid families exceeded the number of identified CPTs, challenging the long-standing one-enzyme-one-product paradigm and suggesting additional, yet unidentified mechanisms regulating chain length. To explore their potential functions, we analyzed the effects of temperature, light, and leaf age on polyisoprenoid accumulation. Environmental treatment had little effect, but leaf aging caused a marked increase in long-chain polyisoprenoids, suggesting roles in development and physiological stability. Our findings reveal new aspects of polyisoprenoid metabolism and highlight their potential functional diversity in plants.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.