Evidence map›Paper›PMID 26216978›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Orthologs of the archaeal isopentenyl phosphate kinase regulate terpenoid production in plants.

Laura K Henry, Michael Gutensohn, Suzanne T Thomas, Joseph P Noel, Natalia Dudareva

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.5field-weighted citation impact, top 7% of its field
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

37 citing papers in PubMed, 98 citations in OpenAlex.

  1. Terpenoids fromPlants (Basel, Switzerland) · 2026
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  15. ACS chemical biology · 2022
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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

5 authors at 3 institutions in 1 country.

Laura K HenryDepartment of Biochemistry, Purdue University, West Lafayette, IN 47907;
Michael GutensohnDepartment of Horticulture and Landscape Architecture, Purdue University, West Lafayette, IN 47907;
Suzanne T ThomasJack H. Skirball Center for Chemical Biology and Proteomics, Salk Institute for Biological Studies, La Jolla, CA 92037;
Joseph P NoelJack H. Skirball Center for Chemical Biology and Proteomics, Salk Institute for Biological Studies, La Jolla, CA 92037; Howard Hughes Medical Institute, Salk Institute for Biological Studies, La Jolla, CA 92037.
Natalia DudarevaDepartment of Biochemistry, Purdue University, West Lafayette, IN 47907; Department of Horticulture and Landscape Architecture, Purdue University, West Lafayette, IN 47907; dudareva@purdue.edu.
Purdue University West Lafayette · USHoward Hughes Medical Institute · USSalk Institute for Biological Studies · US

Funding

Viral Vector Core (VVC)P30CA014195 · NCI · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI Ye Zheng · 1985 to 2026
$82.8M
Howard Hughes Medical Institute
6 · The paper itself

Abstract

Terpenoids, compounds found in all domains of life, represent the largest class of natural products with essential roles in their hosts. All terpenoids originate from the five-carbon building blocks, isopentenyl diphosphate (IPP) and its isomer dimethylallyl diphosphate (DMAPP), which can be derived from the mevalonic acid (MVA) and methylerythritol phosphate (MEP) pathways. The absence of two components of the MVA pathway from archaeal genomes led to the discovery of an alternative MVA pathway with isopentenyl phosphate kinase (IPK) catalyzing the final step, the formation of IPP. Despite the fact that plants contain the complete classical MVA pathway, IPK homologs were identified in every sequenced green plant genome. Here, we show that IPK is indeed a member of the plant terpenoid metabolic network. It is localized in the cytosol and is coexpressed with MVA pathway and downstream terpenoid network genes. In planta, IPK acts in parallel with the MVA pathway and plays an important role in regulating the formation of both MVA and MEP pathway-derived terpenoid compounds by controlling the ratio of IP/DMAP to IPP/DMAPP. IP and DMAP can also competitively inhibit farnesyl diphosphate synthase. Moreover, we discovered a metabolically available carbon source for terpenoid formation in plants that is accessible via IPK overexpression. This metabolite reactivation approach offers new strategies for metabolic engineering of terpenoid production.

Indexed as

ArabidopsisArabidopsis ProteinsArchaeaCytosolGene Expression Regulation, PlantGene Knockout TechniquesGenes, PlantHemiterpenesKineticsMetabolic Networks and PathwaysMevalonic AcidNicotianaOrganophosphorus CompoundsPhosphotransferases (Alcohol Group Acceptor)Plants, Genetically ModifiedPlastids3,3-dimethylallyl pyrophosphateArabidopsis Proteinsfarnesyl pyrophosphategeranyl pyrophosphateHemiterpenesinositol 1,3,4,5,6-pentakisphosphate 2-kinase, Arabidopsisisopentenyl pyrophosphateMevalonic AcidOrganophosphorus CompoundsPhosphotransferases (Alcohol Group Acceptor)Polyisoprenyl PhosphatesSesquiterpenesTerpenesisopentenyl diphosphateisopentenyl phosphate kinaseMEP pathwayMVA pathwayplant terpenoids

Identifiers

PMID26216978
PMCPMC4538610
OpenAlexW2138403893

What OpenQuestion holds

Textmetadata
Read underepoch 390

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 OpenQuestion graph.