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Molecular cloning and expression of  two genes encoding ACCase subunits of Camellia oleifera (Theaceae).

Baoming Wang, Xiaofeng Tan, Jao Jiang and Lin Zhang

The heteromeric acetyl coenzyme A carboxylase (ACCase) in plant seeds catalyzes the formation of malonyl-CoA from acetyl-CoA, which is the rate-limiting step in de novo fatty acid biosynthesis. In this study, we cloned biotin carboxylase (BC) and β-subunits of carboxyltransferase (β-CT) genes of ACCase subunits from Camellia oleifera, namely Co-accC and Co-accD, respectively. The full-length Co-accC (GeneBank accession no.FJ965288) was 1901 bp encoded 530 aa, and the coding regions of Co-accD was 1530 bp encoded 510 aa (accession no. FJ965289), which was in the 2574-bp fragments of rbcL, rbcL-accDintergenic spacer and accD. The comparison of genomic and cDNA sequences showed that they were all intronless. Structural analyses showed that their putative amino acid sequences shared high identity with those of other oil-plants, and that they possessed the ATP-binding site, biotin carboxylation site in the Co-accC protein, and zinc finger motif CX2CX15CX2C in the Co-accD protein. Moreover, transcript expressions of the two genes were carried out in cultivars as well as in tissues and fruit development stages of ‘Huashuo’, the former showed that their expression levels in cultivars were almost correlated with oil contentsof matured seed kernels, the higher expression levels, the higher oil content to some extent, suggesting that they could potentially be as molecular markers for selection of higher oil production cultivars. The latter revealed their expression rules in lipid synthesis and accumulation. Taken together, information from our study indicates that they may be significant in the fatty acid and lipid biosynthesis of seeds, thus be valuable for oil yield of C. oleifera.

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