Abstract
Dinoflagellates make up a diverse array of fatty acids and polyketides. A necessary precursor for their synthesis is malonyl-CoA formed by carboxylating acetyl CoA using the enzyme acetyl-CoA carboxylase (ACC). To date, information on dinoflagellate ACC is limited. Through transcriptome analysis in Amphidinium carterae, we found three full-length homomeric type ACC sequences; no heteromeric type ACC sequences were found. We assigned the putative cellular location for these ACCs based on transit peptide predictions. Using streptavidin Western blotting along with mass spectrometry proteomics, we validated the presence of ACC proteins. Additional bands showing other biotinylated proteins were also observed. Transcript abundance for these ACCs follow the global pattern of expression for dinoflagellate mRNA messages over a diel cycle. This is one of the few descriptions at the transcriptomic and protein level of ACCs in dinoflagellates. This work provides insight into the enzymes which make the CoA precursors needed for fatty acid and toxin synthesis in dinoflagellates.
Highlights
Marine dinoflagellates, a type of phytoplankton, are primary producers in the ecosystem that are of great environmental and economic importance
Biotin carboxylase (BC) is responsible for carboxylating the biotin cofactor, which is transferred to the carboxyl transferase (CT) domain via the biotin carrier protein (BCCP) which serves as an attachment point for the biotin
The ACC1a assembled transcript began with a 144 base 50 untranslated region (UTR), a 6327 base open reading frame (ORF)
Summary
A type of phytoplankton, are primary producers in the ecosystem that are of great environmental and economic importance. Dinoflagellates and algae produce important compounds such as docosahexaenoic acid (DHA) and algal biofuels [4,5]. A necessary protein involved in the production of both fatty acid (FA) products as well as polyketide (PKS) products is acetyl CoA carboxylase (ACC), which produces “activated acetate” units as malonyl CoA [6,7]. ACCs are natively biotinylated proteins that convert acetyl CoA (two carbons) to malonyl CoA (three carbons). Once this conversion occurs, the substrate, malonyl CoA, is committed to go through fatty acid synthase (FAS) or polyketide synthase (PKS) cycles. The CT domain carboxylates the acetyl CoA, converting it to malonyl CoA [6,8]. In the eukaryotic ACC protein there is a large middle domain, the central domain, with no currently defined function [9]
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