Evidence map›Paper›PMID 33089420›Full record

ArticlePlant molecular biology2021

Functional characterization of two type-1 diacylglycerol acyltransferase (DGAT1) genes from rice (Oryza sativa) embryo restoring the triacylglycerol accumulation in yeast.

Rupam Kumar Bhunia, Kshitija Sinha, Kirti Chawla, Vinay Randhawa, Tilak Raj Sharma

Abstract read
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In one paragraph

Article in Plant molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

7 citing papers in PubMed, 13 citations in OpenAlex.

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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 2 institutions in 1 country.

Rupam Kumar BhuniaPlant Tissue Culture and Genetic Engineering, National Agri-Food Biotechnology Institute (NABI), Mohali, Punjab, 140306, India. rupamb2005@gmail.com.ORCID http://orcid.org/0000-0001-7303-5050
Kshitija SinhaPlant Tissue Culture and Genetic Engineering, National Agri-Food Biotechnology Institute (NABI), Mohali, Punjab, 140306, India.
Kirti Chawla *Plant Tissue Culture and Genetic Engineering, National Agri-Food Biotechnology Institute (NABI), Mohali, Punjab, 140306, India.
Vinay Randhawa *Department of Biochemistry, Panjab University, Chandigarh, 160014, India.
Tilak Raj SharmaPlant Tissue Culture and Genetic Engineering, National Agri-Food Biotechnology Institute (NABI), Mohali, Punjab, 140306, India.
National Agri-Food Biotechnology Institute · INPanjab University · IN

Funding

Department of Science and Technology, Ministry of Science and Technology DST/INSPIRE/04/2017/000484Science and Engineering Research Board (IN) CRG/2019/001154
6 · The paper itself

Abstract

key messageTwo OsDGAT1 genes showed the ability to restore TAG and LB synthesis in yeast H1246. Alterations in the N-terminal region of OsDGAT1-1 gene revealed its regulatory role in gene function. Accumulation of triacylglycerol (TAG) or oil in vegetative tissues has emerged as a promising approach to meet the global needs of food, feed, and fuel. Rice (Oryza sativa) has been recognized as an important cereal crop containing nutritional rice bran oil with high economic value for renewable energy production. To identify the key component involved in storage lipid biosynthesis, two type-1 diacylglycerol acyltransferases (DGAT1) from rice were characterized for its in vivo function in the H1246 (dga1, lro1, are1 and are2) yeast quadruple mutant. The ectopic expression of rice DGAT1 (designated as OsDGAT1-1 and OsDGAT1-2) genes restored the capability of TAG synthesis and lipid body (LB) formation in H1246. OsDGAT1-1 showed nearly equal substrate preferences to C16:0-CoA and 18:1-CoA whereas OsDGAT1-2 displayed substrate selectivity for C16:0-CoA over 18:1-CoA, indicating that these enzymes have contrasting substrate specificities. In parallel, we have identified the intrinsically disordered region (IDR) at the N-terminal domains of OsDGAT1 proteins. The regulatory role of the N-terminal domain was dissected. Single point mutations at the phosphorylation sites and truncations of the N-terminal region highlighted reduced lipid accumulation capabilities among different OsDGAT1-1 variants.

Indexed as

Amino Acid SequenceDiacylglycerol O-AcyltransferaseDiglyceridesGene Expression Regulation, DevelopmentalGene Expression Regulation, PlantIntrinsically Disordered ProteinsIsoenzymesLipid DropletsMutationOryzaPhosphorylationPhylogenyPlant ProteinsProtein DomainsRNA, MessengerSaccharomyces cerevisiaeDiacylglycerol O-AcyltransferaseDiglyceridesIntrinsically Disordered ProteinsIsoenzymesPlant ProteinsRNA, MessengerTriglyceridesLipid bodiesPhosphorylationRice (Oryza sativa)Triacylglycerol (TAG)Type-1 diacylglycerol acyltransferases (DGAT1)

Identifiers

PMID33089420
OpenAlexW3094029906

What Socratic holds

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Registered trials

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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.