Evidence map›Paper›PMID 39915980›Full record

ArticleThe Plant journal : for cell and molecular biology2025

The cis-prenyltransferase protein family in Taraxacum koksaghyz.

Boje Müller, Eva Niephaus, Wolfgang Eisenreich, Jan Niklas Bröker, Richard M Twyman, Dirk Prüfer, Christian Schulze Gronover

Abstract read
In one paragraph

Article in The Plant journal : for cell and molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Boje Müller *Fraunhofer Institute for Molecular Biology and Applied Ecology (IME), Johann-Krane-Weg 42, 48149, Münster, Germany.ORCID 0000-0002-3176-0323
Eva Niephaus *Fraunhofer Institute for Molecular Biology and Applied Ecology (IME), Johann-Krane-Weg 42, 48149, Münster, Germany.
Wolfgang EisenreichStructural Membrane Biochemistry, Bavarian NMR Center (BNMRZ), Technical University of Munich (TUM), Lichtenbergstr. 4, 85747, Garching, Germany.
Jan Niklas BrökerFraunhofer Institute for Molecular Biology and Applied Ecology (IME), Johann-Krane-Weg 42, 48149, Münster, Germany.
Richard M TwymanTRM Ltd, PO Box 493, Scarborough, YO11 9FJ, UK.
Dirk PrüferFraunhofer Institute for Molecular Biology and Applied Ecology (IME), Johann-Krane-Weg 42, 48149, Münster, Germany.ORCID 0000-0001-6402-7702
Christian Schulze GronoverFraunhofer Institute for Molecular Biology and Applied Ecology (IME), Johann-Krane-Weg 42, 48149, Münster, Germany.ORCID 0000-0001-6398-2265

Funding

Bundesministerium für Bildung und Forschung 031B0059CDeutsche Forschungsgemeinschaft INST 211/1037-1 LAGG
6 · The paper itself

Abstract

The cis-prenyltransferase (cisPT) enzyme family is involved in diverse biological processes that require the synthesis of linear isoprenoid compounds. Taraxacum koksaghyz is a rubber-producing species and potential crop that has eight cisPT homologs (TkCPT1-8) but their distribution and functions are unclear. We compared the structural organization and sequence homology of the proteins, and defined two groups: TkCPT and TkCPT-like (TkCPTL) proteins that form heteromeric cisPT enzymes (TkCPT1-4), and TkCPT proteins that function as homomeric cisPTs (TkCPT5-8). We found that TkCPT1 and TkCPT2 are predominantly expressed in latex whereas TkCPT3 and TkCPT6-8 are predominantly expressed in leaves. TkCPT4 was constitutively expressed in all T. koksaghyz tissues and TkCPT5 mRNA was detected in flowers. The TkCPT1-4 subunits localized to the endoplasmic reticulum whereas TkCPT5-7 were located in chloroplasts. TkCPT1-4 interacted with TkCPTL1-2, forming heteromeric complexes that complemented yeast lacking cisPT. Homomeric TkCPT6 could also complement yeast lacking cisPT but we observed no cisPT activity for TkCPT5, TkCPT7, or TkCPT8 in yeast functional complementation assays. TkCPT1/TkCPTL1 and TkCPT2/TkCPTL1 expressed in yeast produced extra-long-chain polyisoprenes, whereas TkCPT3/TkCPTL1 and TkCPT4/TkCPTL1 produced long-chain dolichols and polyisoprenes, TkCPT5 and TkCPT6 produced medium-chain polyisoprenes, and TkCPT7 and TkCPT8 catalyzed the formation of nerol. The complexity of cisPT proteins in T. koksaghyz suggests that they synthesize different metabolites in a tissue-specific manner, and thus play distinct roles in isoprenoid metabolism. This is the first comprehensive analysis of the localization, interactions, and products of the entire T. koksaghyz cisPT family in vivo, also revealing a novel pentaprenol found specifically in flowers.

Indexed as

Plant ProteinsTaraxacumTransferasesFlowersGene Expression Regulation, PlantPhylogenyPlant LeavesTerpenescis-prenyl transferasePlant ProteinsTerpenesTransferasesdolichollinear isoprenoidsnatural rubberprotein complexRussian dandelion

Identifiers

PMID39915980
PMCPMC11803133

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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Registered trials

None linked

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.