ArticleScientific reports2022
Reconstitution of prenyltransferase activity on nanodiscs by components of the rubber synthesis machinery of the Para rubber tree and guayule.
Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 17 citations in OpenAlex.
- Ethylene-Enhanced Latex Proteome Is Involved in Stimulation of Natural Rubber Production in the Hevea Rubber Tree.Molecular & cellular proteomics : MCP · 2026Article
- Roles of rubber elongation factor and small rubber particle protein in rubber particles.Plant molecular biology · 2025Review
- Half a Century of Progress: The Evolution of Wheat Germ-Based In Vitro Translation into a Versatile Protein Production Method.International journal of molecular sciences · 2025Review
- Applications of the wheat germ cell-free protein synthesis system in plant biochemical studies.Plant biotechnology (Tokyo, Japan) · 2024Article
- Proteomic and Targeted Lipidomic Analyses of Fluid and Rigid Rubber Particle Membrane Domains in Guayule.Plants (Basel, Switzerland) · 2024Article
- Nanodiscs for the study of membrane proteins.Current opinion in structural biology · 2024Review
- Review
- Transfer mechanism of cell-free synthesized membrane proteins into mammalian cells.Frontiers in bioengineering and biotechnology · 2022Article
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12 authors at 4 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Natural rubber of the Para rubber tree (Hevea brasiliensis) is synthesized as a result of prenyltransferase activity. The proteins HRT1, HRT2, and HRBP have been identified as candidate components of the rubber biosynthetic machinery. To clarify the contribution of these proteins to prenyltransferase activity, we established a cell-free translation system for nanodisc-based protein reconstitution and measured the enzyme activity of the protein-nanodisc complexes. Co-expression of HRT1 and HRBP in the presence of nanodiscs yielded marked polyisoprene synthesis activity. By contrast, neither HRT1, HRT2, or HRBP alone nor a complex of HRT2 and HRBP manifested such activity. Similar analysis of guayule (Parthenium argentatum) proteins revealed that three HRT1 homologs (PaCPT1-3) manifested prenyltransferase activity only when co-expressed with PaCBP, the homolog of HRBP. Our results thus indicate that two heterologous subunits form the core prenyltransferase of the rubber biosynthetic machinery. A recently developed structure modeling program predicted the structure of such heterodimer complexes including HRT1/HRBP and PaCPT2/PaCBP. HRT and PaCPT proteins were also found to possess affinity for a lipid membrane in the absence of HRBP or PaCBP, and structure modeling implicated an amphipathic α-helical domain of HRT1 and PaCPT2 in membrane binding of these proteins.
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