Subcellular localization of dinoflagellate polyketide synthases and fatty acid synthase activity
Article first published online: 5 NOV 2013
© Published 2013. This article is a U.S. Government work and is in the public domain in the U.S.A.
Journal of Phycology
Volume 49, Issue 6, pages 1118–1127, December 2013
How to Cite
Van Dolah, F. M., Zippay, M. L., Pezzolesi, L., Rein, K. S., Johnson, J. G., Morey, J. S., Wang, Z., Pistocchi, R. (2013), Subcellular localization of dinoflagellate polyketide synthases and fatty acid synthase activity. Journal of Phycology, 49: 1118–1127. doi: 10.1111/jpy.12120
- Issue published online: 9 DEC 2013
- Article first published online: 5 NOV 2013
- Accepted manuscript online: 18 SEP 2013 09:16AM EST
- Manuscript Accepted: 25 AUG 2013
- Manuscript Received: 22 MAY 2013
- NOAA/NOS/NCCOS. Grant Number: 02E0025
- NIEHS. Grant Number: S11 ES0 11181
Figure S1. K. brevis PKS protein sequences and location of peptides used for antibody production (squares). A. KS domain protein KB2006, B. KR domain protein KB5299.
Figure S2. Western blot analysis of PKS proteins in O. cf. ovata (O.o.) and C. monotis (C.m.) using: (A.) peptide polyclonal anti-KS against K. brevis KS domain protein KB2006 (left panel) and peptide-blocked anti-KS (right panel), demonstrating specificity of the ~98 kDa band; (B) anti-KR against K. brevis KR domain protein KB2599 (left panel) and peptide-blocked anti-KR (right panel) demonstrating specificity of the ~90 kDa band.
Table S1. K. brevis sequences annotated as PKS or FAS among a database of 65,000 ESTs that assemble into 23,000 contigs. KB2006, KB6736, KB6380, KB4285, and KB1008 are K. brevis KS domain proteins previously described by Monroe and Van Dolah (2008). KB5299 is a KR domain protein.
Please note: Wiley Blackwell is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.