Plant Acetyl-CoA Carboxylase: Structure, Biosynthesis, Regulation, and Gene Manipulation for Plant Breeding

Sasaki, Yukiko; Nagano, Yukio

doi:10.1271/bbb.68.1175

Cited by 359 publications

(301 citation statements)

References 77 publications

(101 reference statements)

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“…Plants have two forms of ACCase; one is present in plastids, catalyzing the de novo synthesis of fatty acids and another in the cytosol, involved in the synthesis of very long-chain fatty acids and secondary metabolites such as flavonoids and anthocyanins. Distinct from other species, where plastid ACCase is composed of four subunits some of which are encoded by chloroplast genes, in grasses both plastid and cytosolic forms of ACCase are encoded by nuclear genes, Acc-1 and Acc-2, respectively (Sasaki and Nagano 2004).…”

Section: Introductionmentioning

confidence: 99%

Single-copy gene fluorescence in situ hybridization and genome analysis: Acc-2 loci mark evolutionary chromosomal rearrangements in wheat

2012

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Section: Introductionmentioning

confidence: 99%

Single-copy gene fluorescence in situ hybridization and genome analysis: Acc-2 loci mark evolutionary chromosomal rearrangements in wheat

2012

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“…Structural models for the plant hetACCase are based on the Escherichia coli homolog. The E. coli hetACCase is composed of two enzymatic subcomplexes: an a/b-CT heterotetramer and a BC/BCCP heterooctamer (Cronan and Waldrop, 2002;Thelen and Ohlrogge, 2002b;Sasaki and Nagano, 2004;). The components of each subcomplex form stable associations, while the two subcomplexes themselves show a relatively weak interaction with one another.…”

Section: Introductionmentioning

confidence: 99%

A Family of Negative Regulators Targets the Committed Step of de Novo Fatty Acid Biosynthesis

et al. 2016

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ORCID ID: 0000-0002-9686-9645 (V.L.)Acetyl-CoA carboxylase (ACCase) catalyzes the committed step of de novo fatty acid biosynthesis. In prokaryotes, green algae, and most plants, this enzyme is a heteromeric complex requiring four different subunits for activity. The plant complex is recalcitrant to conventional purification schemes and hence the structure and composition of the full assembly have been unclear. In vivo coimmunoprecipitation using subunit-specific antibodies identified a novel family of proteins in Arabidopsis thaliana annotated as biotin/lipoyl attachment domain containing (BADC) proteins. Results from yeast two-hybrid and coexpression in Escherichia coli confirmed that all three BADC isoforms interact with the two biotin carboxyl carrier protein (BCCP) isoforms of Arabidopsis ACCase. These proteins resemble BCCP subunits but are not biotinylated due to a mutated biotinylation motif. We demonstrate that BADC proteins significantly inhibit ACCase activity in both E. coli and Arabidopsis. Targeted gene silencing of BADC isoform 1 in Arabidopsis significantly increased seed oil content when normalized to either mass or individual seed. We conclude the BADC proteins are ancestral BCCPs that gained a new function as negative regulators of ACCase after initial loss of the biotinylation motif. A functional model is proposed.

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“…ACCase, a rate-limiting enzyme of FA synthesis, catalyzes the formation of malonyl-CoA from acetylCoA. Subsequently, FAS catalyzes the transfer of the malonyl moiety of malonyl-CoA to acyl-carrier protein (ACP) by adding two carbons to the growing chain, eventually resulting in the formation of C16:0 and C18:0 acyl-ACP, which are then released from the FAS complex and transferred into the cytoplasm (Slabas and Fawcett, 1992;Ohlrogge and Jaworski, 1997;Voelker and Kinney, 2001;Sasaki and Nagano, 2004). In the cytoplasm, FA dehydrogenase (FAD) catalyzes the formation of unsaturated FA, and FA elongase (FAE) sequentially adds two-carbon units to the growing acyl chain to form long-chain FAs.…”

mentioning

confidence: 99%

Enhanced Seed Oil Production in Canola by Conditional Expression of Brassica napus LEAFY COTYLEDON1 and LEC1-LIKE in Developing Seeds

et al. 2011

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The seed oil content in oilseed crops is a major selection trait to breeders. In Arabidopsis (Arabidopsis thaliana), LEAFY COTYLEDON1 (LEC1) and LEC1-LIKE (L1L) are key regulators of fatty acid biosynthesis. Overexpression of AtLEC1 and its orthologs in canola (Brassica napus), BnLEC1 and BnL1L, causes an increased fatty acid level in transgenic Arabidopsis plants, which, however, also show severe developmental abnormalities. Here, we use truncated napin A promoters, which retain the seed-specific expression pattern but with a reduced expression level, to drive the expression of BnLEC1 and BnL1L in transgenic canola. Conditional expression of BnLEC1 and BnL1L increases the seed oil content by 2% to 20% and has no detrimental effects on major agronomic traits. In the transgenic canola, expression of a subset of genes involved in fatty acid biosynthesis and glycolysis is up-regulated in developing seeds. Moreover, the BnLEC1 transgene enhances the expression of several genes involved in Suc synthesis and transport in developing seeds and the silique wall. Consistently, the accumulation of Suc and Fru is increased in developing seeds of the transgenic rapeseed, suggesting the increased carbon flux to fatty acid biosynthesis. These results demonstrate that BnLEC1 and BnL1L are reliable targets for genetic improvement of rapeseed in seed oil production.

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Plant Acetyl-CoA Carboxylase: Structure, Biosynthesis, Regulation, and Gene Manipulation for Plant Breeding

Cited by 359 publications

References 77 publications

Single-copy gene fluorescence in situ hybridization and genome analysis: Acc-2 loci mark evolutionary chromosomal rearrangements in wheat

Single-copy gene fluorescence in situ hybridization and genome analysis: Acc-2 loci mark evolutionary chromosomal rearrangements in wheat

A Family of Negative Regulators Targets the Committed Step of de Novo Fatty Acid Biosynthesis

Enhanced Seed Oil Production in Canola by Conditional Expression of Brassica napus LEAFY COTYLEDON1 and LEC1-LIKE in Developing Seeds

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