Multifunctional acetyl‐CoA carboxylase 1 is essential for very long chain fatty acid elongation and embryo development in <i>Arabidopsis</i>

Baud, Sébastien; Guyon, Virginie; Kronenberger, Jocelyne; Wuillème, Sylvie; Miquel, Martine; Caboche, Michel; Lepiniec, Loïc; Rochat, Christine

doi:10.1046/j.1365-313x.2003.016010.x

Cited by 189 publications

(197 citation statements)

References 52 publications

Supporting

Mentioning

187

Contrasting

Unclassified

Order By: Relevance

“…Because all known mutants in flavonoid synthesis have normal embryos, the absence of VLCFA and their derivatives must be the cause of embryo arrest in acc1 plants (Baud et al, 2003). Interestingly, we detected PvACCase gene promoter-directed GUS activity in the Arabidopsis embryo (Fig.…”

Section: Discussionmentioning

confidence: 78%

See 1 more Smart Citation

Hormonal and Stress Induction of the Gene Encoding Common Bean Acetyl-Coenzyme A Carboxylase

2006

View full text Add to dashboard Cite

Regulation of the cytosolic acetyl-coenzyme A carboxylase (ACCase) gene promoter from common bean (Phaseolus vulgaris) was studied in transgenic Arabidopsis (Arabidopsis thaliana) plants using a β-glucuronidase (GUS) reporter gene fusion (PvACCase∷GUS). Under normal growth conditions, GUS was expressed in hydathodes, stipules, trichome bases, flowers, pollen, and embryos. In roots, expression was observed in the tip, elongation zone, hypocotyl-root transition zone, and lateral root primordia. The PvACCase promoter was induced by wounding, Pseudomonas syringae infection, hydrogen peroxide, jasmonic acid (JA), ethylene, or auxin treatment. Analysis of PvACCase∷GUS expression in JA and ethylene mutants (coronatine insensitive1-1 [coi1-1], ethylene resistant1-1 [etr1-1], coi1-1/etr1-1) suggests that neither JA nor ethylene perception participates in the activation of this gene in response to wounding, although each of these independent signaling pathways is sufficient for pathogen or hydrogen peroxide-induced PvACCase gene expression. We propose a model involving different pathways of PvACCase gene activation in response to stress.

show abstract

Section: Discussionmentioning

confidence: 78%

“…In this context, Baud et al (2003) showed that acc1 mutants displayed defects in embryo development and in VLCFA synthesis. Mutants in the GURKE gene, which encodes ACC1, exhibit embryo defects and its cotyledons are absent or highly reduced (Kajiwara et al, 2004).…”

mentioning

confidence: 99%

Hormonal and Stress Induction of the Gene Encoding Common Bean Acetyl-Coenzyme A Carboxylase

2006

View full text Add to dashboard Cite

show abstract

“…In lower eukaryotes, cytosolic ACC, which is the homolog to animal ACC1, is essential to the viability and development of yeast and the embryos of Arabidopsis (24,33). A null mutation in the acc1 gene of Arabidopsis resulted in embryo lethality, and it was suggested that this lethality is caused by the lack of synthesis of very long-chain fatty acids (33).…”

Section: Discussionmentioning

confidence: 99%

Mutant mice lacking acetyl-CoA carboxylase 1 are embryonically lethal

Abu-Elheiga

Matzuk²,

Kordari³

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

225

162

View full text Add to dashboard Cite

Acetyl-CoA carboxylases (ACC1 and ACC2) catalyze the carboxylation of acetyl-CoA to form malonyl-CoA, an intermediate metabolite that plays a pivotal role in the regulation of fatty acid metabolism. We previously reported that ACC2 null mice are viable, and that ACC2 plays an important role in the regulation of fatty acid oxidation through the inhibition of carnitine palmitoyltransferase I, a mitochondrial component of the fatty-acyl shuttle system. Herein, we used gene targeting to knock out the ACC1 gene. The heterozygous mutant mice (Acc1 ؉/؊ ) had normal fertility and lifespans and maintained a similar body weight to that of their wild-type cohorts. The mRNA level of ACC1 in the tissues of Acc1 ؉/؊ mice was half that of the wild type; however, the protein level of ACC1 and the total malonyl-CoA level were similar. In addition, there was no difference in the acetate incorporation into fatty acids nor in the fatty acid oxidation between the hepatocytes of Acc1 ؉/؊ mice and those of the wild type. In contrast to Acc2 ؊/؊ mice, Acc1 ؊/؊ mice were not detected after mating. Timed pregnancies of heterozygotes revealed that Acc ؊/؊ embryos are already undeveloped at embryonic day (E)7.5, they die by E8.5, and are completely resorbed at E11.5. Our previous results of the ACC2 knockout mice and current studies of ACC1 knockout mice further confirm our hypotheses that malonyl-CoA exists in two independent pools, and that ACC1 and ACC2 have distinct roles in fatty acid metabolism. malonyl-CoAA cetyl-CoA carboxylases (ACCs) are biotin-containing enzymes that catalyze the carboxylation of acetyl-CoA to form malonyl-CoA, an intermediate metabolite that plays a key role in the regulation of fatty acid metabolism. In addition, malonylCoA, as a precursor of the synthesis of long-chain fatty acids, has been implicated as a signal molecule for insulin secretion from the pancreatic ␤-islets (1, 2). The role that ACC plays in energy metabolism in lipogenic tissues (liver and adipose) and in oxidative tissues (liver, heart, and skeletal muscle) have become the focus of many studies (3-8). In lipogenic tissues, malonylCoA is the C 2 -unit donor for de novo synthesis of long-chain fatty acids catalyzed by fatty acid synthase (FAS) and for the chain elongation of fatty acid to very long-chain fatty acids. Moreover, increasing evidence suggests that malonyl-CoA is a regulator of fatty acid oxidation through the inhibition of carnitine palmitoyltransferase I, an enzyme that controls the entry of long-chain fatty acids into the mitochondria for ␤-oxidation (3). In animals, including humans, ACC1 (M r ϭ 265,000) and ACC2 (M r ϭ 280,000) are the two isoforms of acetyl-CoA carboxylase that are encoded by two separate genes, ACC1 and ACC2, respectively, and they display distinct tissue distribution (9-12). ACC1 is abundant in lipogenic tissues, such as liver and adipose tissue, whereas ACC2 is highly expressed in heart, skeletal muscle, and liver (9, 10). Recently, Loftus et al. (13) proposed that malonylCoA plays a role in the central ne...

show abstract

“…Selective herbicides kill grasses such as wheat by specific binding and inhibition of the enzymatic activity in plastids (19), and possibly also in mitochondria (9). Arabidopsis mutants in which the cytosolic ACC gene is disrupted are embryo-lethal and deposit triacylglycerides lacking VLCFAs (20). Finally, all current evidence (8) implicates the ACC reaction as an important regulatory step, controlling metabolite flow during plant development and in response to stress.…”

Section: Discussionmentioning

confidence: 99%

Complex nested promoters control tissue-specific expression of acetyl-CoA carboxylase genes in wheat

Zuther¹,

Huang²,

Jeleńska³

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Cis-acting regulatory elements of the wheat acetyl-CoA carboxylase (ACC) gene family were identified by comparing the promoter activity of 5 end gene fragments fused to a reporter gene in two transient expression systems: wheat protoplasts and epidermal cells of mature embryos. Expression of the plastid and the cytosolic ACC genes is each driven by two nested promoters responsible for the synthesis of two transcript types. The internal promoter is located in an intron removed from transcripts originating at the first promoter. These complex promoters, which are different for the cytosolic and plastid ACC genes, control tissue-specific expression of the enzymatic activity supplying cytosolic, plastid, and mitochondrial pools of malonyl-CoA. The activity of one such complex promoter, driving expression of one of the cytosolic ACC genes, was studied throughout development of transgenic wheat plants carrying a full-length promoter-reporter gene fusion. High activity of the promoter was detected in the coleoptile, in the upper sheath section of the leaf, on the top surface of the ovary, in some sections of the main veins in the lemma and glume, and in abaxial epidermis hair cells of the lemma, glume, and rachis. The findings are consistent with the developmental and environmental requirements for very-long-chain fatty acids and flavonoids, whose synthesis begins with the ACC reaction in the cytosol of these specific cell types.M odern bread wheat has a large hexaploid genome, making molecular genetic studies difficult. We have been studying the structure, evolution, and function of the family of genes encoding the enzyme acetyl-CoA carboxylase (ACC) during wheat development (1-7).In plants, separate ACC isozymes supply the malonyl-CoA pools used for de novo fatty acid (FA) biosynthesis in plastids and mitochondria, and for FA elongation and flavonoid (FL) and stilbene biosynthesis in the cytosol (8, 9). FAs are essential in membrane biogenesis, lipoic acid synthesis, production of oil as storage material, cuticular wax (CW) synthesis, signaling, and pollen-stigma interaction. FLs play multiple roles in plants as pigments and UV protectants, defense compounds, and as signals (10). Malonyl-CoA is also used for protein and smallmolecule malonylation.Our previous study (5) showed that significant regulation of cytosolic and plastid ACC genes in young wheat plants is accomplished at the transcript level. The number and identity of transcribed genes were established by cDNA and genomic DNA sequence comparisons. Transcription start sites and splicing patterns of leader introns were identified for multiple genes, including homoeologs and paralogs. We found that in wheat seedlings, the plastid ACC mRNA level is high in the middle part of the plant and low in roots and leaf blades. The three plastid ACC-homoeologous genes are equivalent in their level of expression. Cytosolic ACC mRNA accumulates to a high level in the lower sheath section of the plant. For the cytosolic ACC genes, we found that transcripts of the three homoeo...

show abstract

Multifunctional acetyl‐CoA carboxylase 1 is essential for very long chain fatty acid elongation and embryo development in Arabidopsis

Cited by 189 publications

References 52 publications

Hormonal and Stress Induction of the Gene Encoding Common Bean Acetyl-Coenzyme A Carboxylase

Hormonal and Stress Induction of the Gene Encoding Common Bean Acetyl-Coenzyme A Carboxylase

Mutant mice lacking acetyl-CoA carboxylase 1 are embryonically lethal

Complex nested promoters control tissue-specific expression of acetyl-CoA carboxylase genes in wheat

Contact Info

Product

Resources

About