A Maize Acetyl-Coenzyme A Carboxylase cDNA Sequence

Egli, Margaret A.; Lutz, Sheila; Somers, David A.; Gengenbach, B. G.

doi:10.1104/pp.108.3.1299

Cited by 25 publications

(9 citation statements)

References 8 publications

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“…No ACCase coding sequence can be found in the complete sequence of rice chloroplast DNA. The plastid ACCase in maize (2) and cytosolic ACCase in wheat, reported here, are nuclear encoded. In other plants, subunits of ACCase other than the carboxyltransferase subunit encoded by a homolog of the Escherichia coli accD gene, present in the chloroplast genome (1,3), must be also encoded in the nuclear DNA.…”

mentioning

confidence: 68%

Structure of a gene encoding a cytosolic acetyl-CoA carboxylase of hexaploid wheat.

Podkowiński¹,

Sroga²,

Haselkorn³

et al. 1996

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

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mentioning

confidence: 68%

Structure of a gene encoding a cytosolic acetyl-CoA carboxylase of hexaploid wheat.

Podkowiński¹,

Sroga²,

Haselkorn³

et al. 1996

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

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“…A 100-amino-acid region (amino acid positions 1±100) at the N-terminal end of the deduced protein contained a high number of hydroxylated and small, hydrophobic amino acids, typical of chloroplast transit peptides (Schlei and Soll 2000). Although the sequences of transit peptides have been reported to be highly variable from one plant to another (Schlei and Soll 2000), the amino acid sequence of this 100-amino-acid region in S. italica showed 89% identity with the transit peptide sequence of the chloroplastic ACCase from maize (Egli et al 1995), thus strongly supporting this conclusion. The four most conserved amino acid regions among eukaryotic-type ACCases, the biotin-carboxylase domain, the biotin-carboxyl carrier domain and the b-and a-domains of the CT (Gornicki et al 1994), are located at amino acid positions 136±633, 662±841, 1658±1707 and 1936±1969, respectively.…”

Section: Structure Of S Italica Chloroplastic Accasementioning

confidence: 93%

An isoleucine-leucine substitution in chloroplastic acetyl-CoA carboxylase from green foxtail (Setaria viridis L. Beauv.) is responsible for resistance to the cyclohexanedione herbicide sethoxydim

Délye

Wang

Darmency

2001

Planta

104

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The cDNAs encoding chloroplastic acetyl-CoA carboxylase (ACCase, EC 6.4.1.2) from three lines of Setaria viridis (L. Beauv.) resistant or sensitive to sethoxydim, and from one sethoxydim-sensitive line of Setaria italica (L. Beauv.) were cloned and sequenced. Sequence comparison revealed that a single isoleucine-leucine substitution discriminated ACCases from sensitive and resistant lines. Using near-isogenic lines of S. italica derived from interspecific hybridisation, we demonstrated that the transfer of the S. viridis mutant ACCase allele into a sethoxydim-sensitive S. italica line conferred resistance to this herbicide. We confirmed this result using allele-specific polymerase chain reaction and showed that a single copy of the mutant allele is sufficient to confer resistance to sethoxydim. We conclude that a mutant allele of chloroplastic ACCase encoding a leucine residue instead of an isoleucine residue at position 1780 is a major gene of resistance to sethoxydim.

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“…The isolation and characterization of ACCases have been reported in A. thaliana (Roesler et al 1994;Yanai et al 1995;Sun et al 1997;Ke et al 2000), B. napus (Elborough et al 1996;Schulte et al 1994;Schulte et al 1997), Glycine max (Reverdatto et al 1999), Pisum sativum (Sasaki et al 1993;Shorrosh et al 1996;Kozaki et al 2001), Medicago sativa , Nicotiana tabacum (Shorrosh et al 1995), Solanum tuberosum (Lee et al 2004), Triticum aestivum (Podkowinski et al 1996;Gornicki et al 1997;Chalupska et al 2008), and Zea mays (Egli et al 1995). Peanut is widely grown and ranks fifth among the world oil production crops (Moretzsohn et al 2004).…”

Section: Introductionmentioning

confidence: 97%

Isolation and Characterization of Putative Acetyl-CoA Carboxylases in Arachis hypogaea L.

Xia

Zhao

et al. 2009

Plant Mol Biol Rep

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Candidate genes of multisubunit (MS) and multifunctional (MF) acetyl-CoA carboxylase (ACCase) including accB1, accB2, accC, accA, accD, and MF-ACCase were isolated from peanut by sequencing a full-length cDNA library and homology-based cloning. Primary structures of peanut ACCases were highly conserved, especially biochemical function domains, compared with other higher plants and Escherichia coli. The numbers of homologs of each ACCase gene expressed in developing seed of peanut varied from two to five. Two editing sites of peanut accD were identified by comparing genomic DNA and its corresponding cDNAs. The MS-ACCase of Arachis hypogaea and Arabidopsis thaliana shared a conservative structure of gene organization. Semiquantitative reverse transcription polymerase chain reaction analysis indicated that MS-ACCase and MF-ACCase genes were expressed in all peanut tissues examined, but their mRNA expression level were quite different. In peanut seed development, accC, accA, accD, and MF-ACCase mRNAs were expressed strongly at 60 days after pegging.

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A Maize Acetyl-Coenzyme A Carboxylase cDNA Sequence

Cited by 25 publications

References 8 publications

Structure of a gene encoding a cytosolic acetyl-CoA carboxylase of hexaploid wheat.

Structure of a gene encoding a cytosolic acetyl-CoA carboxylase of hexaploid wheat.

An isoleucine-leucine substitution in chloroplastic acetyl-CoA carboxylase from green foxtail (Setaria viridis L. Beauv.) is responsible for resistance to the cyclohexanedione herbicide sethoxydim

Isolation and Characterization of Putative Acetyl-CoA Carboxylases in Arachis hypogaea L.

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