@ARTICLE{TreeBASE2Ref24484,
author = {Tsvetan Radoslavov Bachvaroff and Ernest P Williams and Rosemary Jagus and Allen R Place},
title = {A noncryptic noncanonical multi-module PKS/NRPS found in dinoflagellates},
year = {2015},
keywords = {polyketide, non-ribosomal peptide synthase, dinoflagellate, Burkholderia},
doi = {},
url = {http://},
pmid = {},
journal = {Proceedings of the 16th International Conference on Harmful Algae. International Society for the Study of Harmful Algae 2015},
volume = {},
number = {},
pages = {},
abstract = {Dinoflagellates produce a variety of compounds, likely using polyketide synthases (PKS) or non-ribosomal peptide synthases (NRPS) based on structure and labeling studies. An 8 domain hybrid PKS/NRPS greater than 8 thousand bases was identified in 19 deeply sequenced dinoflagellate transcriptomes. The gene was found in data from Oxyrrhis marina and 18 core dinoflagellates, but not the syndinean genus Amoebophrya. Spliced leaders, introns, and multiple subtle sequence variants were found, ruling out bacterial contaminants and confirming the dinoflagellate source of the sequences. However, the domain content and order are shared with a bacterial cryptic noncanonical PKS/NRPS (BurA) from Burkholderia spp., indicating a likely bacterial origin through horizontal gene transfer. The dinoflagellate and bacterial genes also have similar amino acid and malonyl CoA binding pockets. Based on labeling studies from Burkholderia spp. the dinoflagellates may use methionine to produce a propionate for incorporation into natural products.}
}
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Citation title: "A noncryptic noncanonical multi-module PKS/NRPS found in dinoflagellates".
