Putative monofunctional type I polyketide synthase units: a dinoflagellate-specific feature?

PLoS One. 2012;7(11):e48624. doi: 10.1371/journal.pone.0048624. Epub 2012 Nov 5.

Abstract

Marine dinoflagellates (alveolata) are microalgae of which some cause harmful algal blooms and produce a broad variety of most likely polyketide synthesis derived phycotoxins. Recently, novel polyketide synthesase (PKS) transcripts have been described from the Florida red tide dinoflagellate Karenia brevis (gymnodiniales) which are evolutionarily related to Type I PKS but were apparently expressed as monofunctional proteins, a feature typical of Type II PKS. Here, we investigated expression units of PKS I-like sequences in Alexandrium ostenfeldii (gonyaulacales) and Heterocapsa triquetra (peridiniales) at the transcript and protein level. The five full length transcripts we obtained were all characterized by polyadenylation, a 3' UTR and the dinoflagellate specific spliced leader sequence at the 5'end. Each of the five transcripts encoded a single ketoacylsynthase (KS) domain showing high similarity to K. brevis KS sequences. The monofunctional structure was also confirmed using dinoflagellate specific KS antibodies in Western Blots. In a maximum likelihood phylogenetic analysis of KS domains from diverse PKSs, dinoflagellate KSs formed a clade placed well within the protist Type I PKS clade between apicomplexa, haptophytes and chlorophytes. These findings indicate that the atypical PKS I structure, i.e., expression as putative monofunctional units, might be a dinoflagellate specific feature. In addition, the sequenced transcripts harbored a previously unknown, apparently dinoflagellate specific conserved N-terminal domain. We discuss the implications of this novel region with regard to the putative monofunctional organization of Type I PKS in dinoflagellates.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Catalytic Domain
  • Conserved Sequence
  • Dinoflagellida / enzymology*
  • Evolution, Molecular
  • Molecular Sequence Data
  • Phylogeny
  • Polyketide Synthases / chemistry
  • Polyketide Synthases / genetics
  • Polyketide Synthases / metabolism*
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Species Specificity

Substances

  • Polyketide Synthases

Grants and funding

Financial support was provided by the PACES research program of the Alfred Wegener Institute, within the Helmholtz Foundation Initiative in Earth and Environment. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.