Investigating a multi-domain polyketide synthase in Amphidinium carterae

Simple item page
dc.contributor.authorHaq, Saddef
dc.contributor.authorOyler, Benjamin L.
dc.contributor.authorWilliams, Ernest
dc.contributor.authorKhan, Mohd M.
dc.contributor.authorGoodlett, David R.
dc.contributor.authorBachvaroff, Tsvetan
dc.contributor.authorPlace, Allen R.
dc.date.accessioned2024-01-23T23:20:32Z
dc.date.available2024-01-23T23:20:32Z
dc.date.copyright2023en_US
dc.date.issued2023
dc.description.abstractDinoflagellates are unicellular organisms that are implicated in harmful algal blooms (HABs) caused by potent toxins that are produced through polyketide synthase (PKS) pathways. However, the exact mechanisms of toxin synthesis are unknown due to a lack of genomic segregation of fat, toxins, and other PKS-based pathways. To better understand the underlying mechanisms, the actions and expression of the PKS proteins were investigated using the toxic dinoflagellate Amphidinium carterae as a model. Cerulenin, a known ketosynthase inhibitor, was shown to reduce acetate incorporation into all fat classes with the toxins amphidinol and sulpho-amphidinol. The mass spectrometry analysis of cerulenin-reacted synthetic peptides derived from ketosynthase domains of A. carterae multimodular PKS transcripts demonstrated a strong covalent bond that could be localized using collision-induced dissociation. One multi-modular PKS sequence present in all dinoflagellates surveyed to date was found to lack an AT domain in toxin-producing species, indicating trans-acting domains, and was shown by Western blotting to be post-transcriptionally processed. These results demonstrate how toxin synthesis in dinoflagellates can be differentiated from fat synthesis despite common underlying pathway.en_US
dc.description.reviewstatusRevieweden_US
dc.description.scholarlevelFacultyen_US
dc.description.sponsorshipThis work was funded by grants from Oceans & Human Health NIH, R01ES021949-01/NSF OCE1313888 for R.J. and A.R.P. This work was also funded in part by a grant from NOAA-NOS-NCCOS-2012-2002987 to A.R.P.en_US
dc.identifier.citationHaq, S., Oyler, B. L., Williams, E., Khan, M. M., Goodlett, D. R., Bachvaroff, T., & Place, A. R. (2023). Investigating a multi-domain polyketide synthase in Amphidinium carterae. Marine Drugs, 21(8), 425. https://doi.org/10.3390/md21080425en_US
dc.identifier.urihttps://doi.org/10.3390/md21080425
dc.identifier.urihttp://hdl.handle.net/1828/15852
dc.language.isoenen_US
dc.publisherMarine Drugsen_US
dc.subjectdinoflagellate
dc.subjectPKS
dc.subjectcerulenin
dc.subjecttoxin
dc.subject.departmentDepartment of Biochemistry and Microbiology
dc.titleInvestigating a multi-domain polyketide synthase in Amphidinium carteraeen_US
dc.typeArticleen_US

Files

Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
haq_saddef_mar drugs_2023.pdf
Size:
3.7 MB
Format:
Adobe Portable Document Format
Description:
Download
License bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
2 KB
Format:
Item-specific license agreed upon to submission
Description:
Download

Collections

Faculty and Staff Publications
 
University of Victoria Libraries

We acknowledge and respect the Lək̓ʷəŋən (Songhees and Esquimalt) Peoples on whose territory the university stands, and the Lək̓ʷəŋən and W̱SÁNEĆ Peoples whose historical relationships with the land continue to this day.