Evidence map›Paper›PMID 41166573›Full record

ArticlePlant physiology2025

Complete replacement of Arabidopsis oil-producing enzymes with heterologous diacylglycerol acyltransferases.

Sean T McGuire, Jay Shockey, Alexandra Richards, Andrei Smertenko, Philip D Bates

Abstract read
In one paragraph

Article in Plant physiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Review
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.

Sean T McGuireInstitute of Biological Chemistry, Washington State University, Pullman, WA 99164, USA.ORCID 0000-0002-5629-7873
Jay ShockeyUnited States Department of Agriculture, Agricultural Research Service, Southern Regional Research Service, 1100 Allen Toussaint Blvd, New Orleans, LA 70124, USA.ORCID 0000-0002-5057-5457
Alexandra RichardsInstitute of Biological Chemistry, Washington State University, Pullman, WA 99164, USA.
Andrei SmertenkoInstitute of Biological Chemistry, Washington State University, Pullman, WA 99164, USA.ORCID 0000-0002-5078-4881
Philip D BatesInstitute of Biological Chemistry, Washington State University, Pullman, WA 99164, USA.ORCID 0000-0002-1291-3363

Funding

Agriculture and Food Research Initiative Competitive Grants Program FoundationalApplied Science Program 2023-67013-39022Hatch Project #1015621Multi-State Project #1013013National Institute of Food and AgricultureNational Science Foundation NSF-MCB 2242822Office of Biological and Environmental Research DE-SC0023142U.S. Department of Agriculture
6 · The paper itself

Abstract

Acyl-CoA:diacylglycerol acyltransferase 1 (DGAT1) and phospholipid:diacylglycerol acyltransferase 1 (PDAT1) share responsibility for triacylglycerol (TAG) biosynthesis, and their selectivities control TAG fatty acid (FA) compositions. For rational metabolic engineering of seed oils, replacing endogenous TAG biosynthesis with exogenous enzymes containing different substrate FA selectivities is desirable; however, the dgat1-1/pdat1-2 double mutant is pollen lethal. Here, we evaluated the ability of 3 DGAT1s, from phylogenetically diverse plants with distinct TAG assembly processes, to completely replace endogenous TAG biosynthesis in Arabidopsis (Arabidopsis thaliana). We transformed dgat1-1 mutant plants with expression constructs for DGAT1s from Camelina sativa, Physaria fendleri, and castor (Ricinus communis). Transgene expression was properly "contextualized" by using a previously determined minimum necessary expression unit containing the promoter/5' UTR and first intron of native AtDGAT1; both of these DNA elements are essential for pollen expression. Next, we crossed homozygous lines with a DGAT1/DGAT1/PDAT1/pdat1-2 parent. C. sativa and P. fendleri DGAT1s restored the FA compositions and transcriptional differences of dgat1-1 to near wild-type and rescued the dgat1-1/pdat1-2 pollen lethality. R. communis DGAT1 was active in dgat1-1 seeds but produced unique oil profiles and alterations in the expression of lipid metabolic genes; it also failed to rescue dgat1-1/pdat1-2 lethality. This study confirms that the promoter and first intron of AtDGAT1 can modulate the expression of foreign DGAT1 genes to fit the correct spatiotemporal profile necessary for completely replacing endogenous TAG biosynthesis. Furthermore, it demonstrates an additional layer of unexpected enzyme incompatibility between oilseed lineages, which may complicate bioengineering approaches that seek to replace essential genes with orthologs.

Indexed as

ArabidopsisArabidopsis ProteinsDiacylglycerol O-AcyltransferasePlant OilsAcyltransferasesFatty AcidsGene Expression Regulation, PlantPlants, Genetically ModifiedRicinusSeedsTriglyceridesAcyltransferasesArabidopsis ProteinsDGAT1 protein, ArabidopsisDiacylglycerol O-AcyltransferaseFatty AcidsPDAT1 protein, ArabidopsisPlant OilsTriglycerides

Identifiers

PMID41166573
PMCPMC12612817

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.