Journal
MOLECULAR PHYLOGENETICS AND EVOLUTION
Volume 168, Issue -, Pages -Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ympev.2022.107417
Keywords
Alexandrium; Evolutionary event; Toxic dinoflagellate; Saxitoxin; sxtA
Funding
- National Research Foundation of Korea (NRF) - Korea government (MSIT) [2020R1A2C2013373]
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By studying the sxtA gene sequences of two toxic dinoflagellates, it was found that there are differences in their gene coding structure and evolutionary history. The evolution of sxtA in Alexandrium may involve acquiring specific domains, which significantly affect toxin biosynthesis.
Marine dinoflagellates Alexandrium are known to produce saxitoxin (STX) and cause paralytic shellfish poisoning (PSP) which can result in mortality in human. SxtA is considered a core gene for the biosynthesis of STX. However, its gene coding structure and evolutionary history have yet to be fully elucidated. Here, we determined the full-length sequences of sxtA cDNA and genomic coding regions from two toxic dinoflagellates, Alexandrium catenella (LIMS-PS-2645 and LIMS-PS-2647) and A. pacificum (LMBE-C4), characterised their domain structures, and resolved evolutionary events. The sxtA gene was encoded on the genome without introns, and was identical in length (4002 bp) between two A. catenella strains, but their sequences differed from A. pacificum (5031 bp). SxtA consists of four domains, sxtA1, sxtA2, sxtA3, and sxtA4; however, A. pacificum has an extra domain TauD near sxtA1. Each domain had >64.4% GC content, with the highest being 71.6% in sxtA3. Molecular divergence was found to be significantly higher in sxtA4 than in the other domains. Phylogenetic trees of sxtA and separate domains showed that bacteria diverged earliest, followed by non-toxic, toxic cyanobacteria, toxic dinoflagellates. While sxtA domains in Alexandrium were similar to the PKS-like structure with the conserved sxtA1, sxtA2, and sxtA3. PKS_KS may be replaced by sxtA4 in toxic Alexandrium. These suggest that sxtA in Alexandrium may have evolved by acquiring specific domains, whose modification and complexity markedly affect toxin biosynthesis.
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