Wheat acetyl-coenzyme A carboxylase: cDNA and protein structure.

Górnicki, Piotr; Podkowiński, Jan; Scappino, Lori; DiMaio, J. Michael; Ward, Eric; Haselkorn, Robert

doi:10.1073/pnas.91.15.6860

Cited by 72 publications

(54 citation statements)

References 32 publications

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“…The highly conserved biotin carboxylase domain is located near the N terminus of all eukaryotic-type multidomain ACCs (15,18). In plant cytosolic ACCs, this domain is preceded by only 20 aa.…”

Section: T Gondii Accs and Theirmentioning

confidence: 99%

Subcellular localization of acetyl-CoA carboxylase in the apicomplexan parasite Toxoplasma gondii

Jeleńska

Crawford

Harb

et al. 2001

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

107

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Apicomplexan parasites such as Toxoplasma gondii contain a primitive plastid, the apicoplast, whose genome consists of a 35-kb circular DNA related to the plastid DNA of plants. Plants synthesize fatty acids in their plastids. The first committed step in fatty acid synthesis is catalyzed by acetyl-CoA carboxylase (ACC). This enzyme is encoded in the nucleus, synthesized in the cytosol, and transported into the plastid. In the present work, two genes encoding ACC from T. gondii were cloned and the gene structure was determined. Both ORFs encode multidomain proteins, each with an N-terminal extension, compared with the cytosolic ACCs from plants. The N-terminal extension of one isozyme, ACC1, was shown to target green fluorescent protein to the apicoplast of T. gondii . In addition, the apicoplast contains a biotinylated protein, consistent with the assertion that ACC1 is localized there. The second ACC in T. gondii appears to be cytosolic. T. gondii mitochondria also contain a biotinylated protein, probably pyruvate carboxylase. These results confirm the essential nature of the apicoplast and explain the inhibition of parasite growth in cultured cells by herbicides targeting ACC.

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Section: T Gondii Accs and Theirmentioning

confidence: 99%

Subcellular localization of acetyl-CoA carboxylase in the apicomplexan parasite Toxoplasma gondii

Jeleńska

Crawford

Harb

et al. 2001

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

107

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show abstract

“…Six different sequences of the Acc-2 gene and pseudogene are present in the wheat genome (Podkowinski et al 1996;Huang et al 2002); at least three of the Acc-2 genes are expressed equally in young leaves (Podkowinski et al 2003) and their coding sequences (6.3 kb) have 98% identity (Gornicki et al 1994;Chalupska et al 2008). The genes and pseodogenes are likely arranged in tandem repeats (Faris et al 2001).…”

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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“…In most plant species, chloroplastic ACCase is a multisubunit enzyme, the subunits of which are encoded in the nDNA, except the ␤-subunit of CT that is encoded by a chloroplastic gene (Konishi et al, 1996). However, in Poaceae (grasses), the chloroplastic ACCase is a multidomain enzyme (Konishi et al, 1996) encoded by a nuclear gene distinct from that coding for the cytosolic ACCase isoform (Gornicki et al, 1994Podkowinski et al, 1996).…”

mentioning

confidence: 99%

An Isoleucine Residue within the Carboxyl-Transferase Domain of Multidomain Acetyl-Coenzyme A Carboxylase Is a Major Determinant of Sensitivity to Aryloxyphenoxypropionate But Not to Cyclohexanedione Inhibitors

et al. 2003

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A 3,300-bp DNA fragment encoding the carboxyl-transferase domain of the multidomain, chloroplastic acetyl-coenzyme A carboxylase (ACCase) was sequenced in aryloxyphenoxypropionate (APP)-resistant and -sensitive Alopecurus myosuroides (Huds.). No resistant plant contained an Ile-1,781-Leu substitution, previously shown to confer resistance to APPs and cyclohexanediones (CHDs). Instead, an Ile-2,041-Asn substitution was found in resistant plants. Phylogenetic analysis of the sequences revealed that Asn-2,041 ACCase alleles derived from several distinct origins. Allele-specific polymerase chain reaction associated the presence of Asn-2,041 with seedling resistance to APPs but not to CHDs. ACCase enzyme assays confirmed that Asn-2,041 ACCase activity was moderately resistant to CHDs but highly resistant to APPs. Thus, the Ile-2,041-Asn substitution, which is located outside a domain previously shown to control sensitivity to APPs and CHDs in wheat (Triticum aestivum), is a direct cause of resistance to APPs only. In known multidomain ACCases, the position corresponding to the Ile/Asn-2,041 residue in A. myosuroides is occupied by an Ile or a Val residue. In Lolium rigidum (Gaud.), we found Ile-Asn and Ile-Val substitutions. The Ile-Val change did not confer resistance to the APP clodinafop, whereas the Ile-Asn change did. The position and the particular substitution at this position are of importance for sensitivity to APPs.

show abstract

Wheat acetyl-coenzyme A carboxylase: cDNA and protein structure.

Cited by 72 publications

References 32 publications

Subcellular localization of acetyl-CoA carboxylase in the apicomplexan parasite Toxoplasma gondii

Subcellular localization of acetyl-CoA carboxylase in the apicomplexan parasite Toxoplasma gondii

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

An Isoleucine Residue within the Carboxyl-Transferase Domain of Multidomain Acetyl-Coenzyme A Carboxylase Is a Major Determinant of Sensitivity to Aryloxyphenoxypropionate But Not to Cyclohexanedione Inhibitors

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