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- Title
Ketoacyl synthase domain is a major determinant for fatty acyl chain length in <i>Saccharomyces cerevisiae</i>.
- Authors
Sangwallek, Juthaporn; Kaneko, Yoshinobu; Sugiyama, Minetaka; Ono, Hisayo; Bamba, Takeshi; Fukusaki, Eiichiro; Harashima, Satoshi
- Abstract
Yeast fatty acid synthase (Fas) comprises two subunits, α 6 and β 6, encoded by FAS2 and FAS1, respectively. To determine features of yeast Fas that control fatty acyl chain length, chimeric genes were constructed by combining FAS sequences from Saccharomyces cerevisiae ( ScFAS) and Hansenula polymorpha ( HpFAS), which mostly produces C16 and C18 fatty acids, respectively. The C16/C18 ratios decreased from 2.2 ± 0.1 in wild-type S. cerevisiae to 1.0 ± 0.1, 0.5 ± 0.2 and 0.8 ± 0.1 by replacement of ScFAS1, ScFAS2 and ScFAS1 ScFAS2 with HpFAS1, HpFAS2 and HpFAS1 HpFAS2, respectively, suggesting that the α, but not β subunits play a major role in determining fatty acyl chain length. Replacement of phosphopantetheinyl transferase (PPT) domain with the equivalent region from HpFAS2 did not affect C16/C18 ratio. Chimeric Fas2 containing half N-terminal ScFas2 and half C-terminal HpFas2 carrying H. polymorpha ketoacyl synthase (KS) and PPT gave a remarkable decrease in C16/C18 ratio (0.6 ± 0.1), indicating that KS plays a major role in determining chain length.
- Subjects
FATTY-acyl-CoA; CHAIN length (Chemistry); SACCHAROMYCES cerevisiae; FATTY acid synthases; YEAST; FUNGAL genetics
- Publication
Archives of Microbiology, 2013, Vol 195, Issue 12, p843
- ISSN
0302-8933
- Publication type
Article
- DOI
10.1007/s00203-013-0933-3