A rapeseed FAE1 gene is linked to the E1 locus associated with variation in the content of erucic acid

Barret, P.; Delourme, Régine; Renard, M.; Domergue, Frédéric; Lessire, René; Delseny, Michel; Roscoe, Thomas

doi:10.1007/s001220050725

Cited by 105 publications

(90 citation statements)

References 22 publications

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“…was in good agreement with lengths of the FAE1s of B. napus and Arabidopsis (James et al, 1995;Barret et al, 1998;Fourmann et al, 1998). The predicted polypeptide of 507 amino acids encoded by the FAE1 allele E 1 also showed high similarity with the proteins encoded by the FAE1s in B. juncea (97% identity), B. napus (96% identity), B. rapa (96% identity), B. oleracea (96% identity), and Arabidopsis (86% identity) (Supplemental Figure 1).…”

Section: Discussionsupporting

confidence: 64%

Transposable Element Insertion and Epigenetic Modification Cause the Multiallelic Variation in the Expression of FAE1 in Sinapis alba

Zeng

Cheng

2014

The Plant Cell

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Naturally occurring heritable variation provides a fundamental resource to reveal the genetic and molecular bases of traits in forward genetic studies. Here, we report the molecular basis of the differences in the four alleles E 1 , E 2 , E 3 , and e of the FATTY ACID ELONGATION1 (FAE1) gene controlling high, medium, low, and zero erucic content in yellow mustard (Sinapis alba). E 1 represents a fully functional allele with a coding DNA sequence (CDS) of 1521 bp and a promoter adjacent to the CDS. The null allele e resulted from an insertional disruption in the CDS by Sal-PIF, a 3100-bp PIF/Harbinger-like DNA transposon, whereas E 2 and E 3 originated from the insertion of Sal-T1, a 4863-bp Copia-like retrotransposon, in the 59 untranslated region. E 3 was identical to E 2 but showed cytosine methylation in the promoter region and was thus an epiallele having a further reduction in expression. The coding regions of E 2 and E 3 also contained five single-nucleotide polymorphisms (SNPs) not present in E 1 , but expression studies in Saccharomyces cerevisiae indicated that these SNPs did not affect enzyme functionality. These results demonstrate a comprehensive molecular framework for the interplay of transposon insertion, SNP/indel mutation, and epigenetic modification influencing the broad range of natural genetic variation in plants.

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Section: Discussionsupporting

confidence: 64%

Transposable Element Insertion and Epigenetic Modification Cause the Multiallelic Variation in the Expression of FAE1 in Sinapis alba

Zeng

Cheng

2014

The Plant Cell

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“…The progeny of a cross between the varieties B002 (Ͻ1% erucic acid) and Hokkaido (Ͼ50% erucic acid) of oilseed rape (Brassica napus) described in Barret et al (1998) were used for the construction of cDNA libraries and the isolation of the BAT2 gene. For the mapping studies we used the double-haploid population, which was derived from the cross between the varieties Darmor-bzh (Ͻ1% erucic acid) and Yudal (Ͼ50% erucic acid) and was used for the construction of a genetic map of B. napus (Foisset et al, 1996).…”

Section: Plant Materialsmentioning

confidence: 99%

“…The construction of an immature embryo cDNA library of B. napus in the vector Lambda ZAP II (Stratagene) as described in Barret et al (1998). An aliquot representative of the primary library was subjected to in vivo excision using the ExAssist system (Stratagene).…”

Section: Isolation Of B Napus Cdnas By Heterologous Complementationmentioning

confidence: 99%

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A Plastidial Lysophosphatidic Acid Acyltransferase from Oilseed Rape1

et al. 1999

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The biosynthesis of phosphatidic acid, a key intermediate in the biosynthesis of lipids, is controlled by lysophosphatidic acid (LPA, or 1-acyl-glycerol-3-P) acyltransferase (LPAAT, EC 2.3.1.51). We have isolated a cDNA encoding a novel LPAAT by functional complementation of the Escherichia coli mutant plsC with an immature embryo cDNA library of oilseed rape (Brassica napus). Transformation of the acyltransferase-deficient E. coli strain JC201 with the cDNA sequence BAT2 alleviated the temperature-sensitive phenotype of the plsC mutant and conferred a palmitoyl-coenzyme A-preferring acyltransferase activity to membrane fractions. The BAT2 cDNA encoded a protein of 351 amino acids with a predicted molecular mass of 38 kD and an isoelectric point of 9.7. Chloroplast-import experiments showed processing of a BAT2 precursor protein to a mature protein of approximately 32 kD, which was localized in the membrane fraction. BAT2 is encoded by a minimum of two genes that may be expressed ubiquitously. These data are consistent with the identity of BAT2 as the plastidial enzyme of the prokaryotic glycerol-3-P pathway that uses a palmitoyl-ACP to produce phosphatidic acid with a prokaryotictype acyl composition. The homologies between the deduced protein sequence of BAT2 with prokaryotic and eukaryotic microsomal LAP acytransferases suggest that seed microsomal forms may have evolved from the plastidial enzyme.Phosphatidic acid is a key intermediate in the biosynthesis of phospho-and glycerolipids, essential components of all cellular membranes and of triacylglycerols. In most plant species, palmitoyl-ACP and oleoyl-ACP are the predominant products of de novo fatty acid biosynthesis in the chloroplast (Ohlrogge et al., 1993). These fatty acids may enter the prokaryotic pathway of lipid biosynthesis by transfer of the acyl group from ACP to glycerol-3-P, which is mediated by a stromal glycerol-3-P acyltransferase to form LPA or to position sn-2 of glycerol-3-P mediated by LPAAT (EC 2.3.1.51) to form phosphatidic acid. The phosphatidic acid produced by the prokaryotic pathway of the chloroplast is then used to produce phosphatidylglycerol (for review, see Ohlrogge and Browse, 1995) or is dephosphorylated to diacylglycerol, from which the glycodiacylglycerols characteristic of the thylakoid membrane are derived (for review, see Douce and Joyard, 1990).Alternatively, the elongation of fatty acids may be terminated by the action of an acyl-ACP thioesterase, which hydrolyzes the acyl-ACP to release a free fatty acid, which then leaves the plastid. The fatty acid in the form of an acyl-CoA thioester may participate in the synthesis of glycerolipids via the eukaryotic pathway located at the ER. The phosphatidic acid of the cytoplasmic pathway is used to produce the phospholipids characteristic of extrachloroplastic lipids. The phosphatidylcholine produced by the eukaryotic pathway is a substrate for desaturation, after which the diacylglycerol moiety may be returned to the chloroplast. The contribution of each pathway to the syn...

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“…Mutations in FAE1 resulted in reduced levels of seed VLCFAs [67,68], and a deficiency in acyl chain elongation activities toward C 18 and C 20 FAs [69]. FAE1 homologs were identified in several plants, Brassica oleracea [70], Brassica campestris [71], Brassica oleacea [71], Simmondsia chinensis [72], Lesquerella fendleri [73] and Limnanthes alba [74] and also in the green algae, Dunaliella salina [75]. In the Arabidopsis genome, 20 predicted FAE1 homologs were found (Fig.…”

Section: Fatty Acid Elongase-3 Ketoacyl Coa Synthases (Fae-3kcss)mentioning

confidence: 99%

Characterization of Enzymes Involved in Fatty Acid Elongation

Paul¹

2007

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A rapeseed FAE1 gene is linked to the E1 locus associated with variation in the content of erucic acid

Cited by 105 publications

References 22 publications

Transposable Element Insertion and Epigenetic Modification Cause the Multiallelic Variation in the Expression of FAE1 in Sinapis alba

Transposable Element Insertion and Epigenetic Modification Cause the Multiallelic Variation in the Expression of FAE1 in Sinapis alba

A Plastidial Lysophosphatidic Acid Acyltransferase from Oilseed Rape1

Characterization of Enzymes Involved in Fatty Acid Elongation

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