A critical role for very long-chain fatty acid elongases in oleic acid-mediated Saccharomyces cerevisiae cytotoxicity

2018 ◽  
Vol 207 ◽  
pp. 1-7 ◽  
Author(s):  
Qiao Wang ◽  
Xiuxiu Du ◽  
Ke Ma ◽  
Ping Shi ◽  
Wenbin Liu ◽  
...  
1988 ◽  
Vol 177 (1) ◽  
pp. 207-211 ◽  
Author(s):  
Jean-Jacques BESSOULE ◽  
Rene LESSIRE ◽  
Michel RIGOULET ◽  
Bernard GUERIN ◽  
Claude CASSAGNE

2017 ◽  
Vol 8 (1) ◽  
Author(s):  
Tao Yu ◽  
Yongjin J. Zhou ◽  
Leonie Wenning ◽  
Quanli Liu ◽  
Anastasia Krivoruchko ◽  
...  

Abstract Production of chemicals and biofuels through microbial fermentation is an economical and sustainable alternative for traditional chemical synthesis. Here we present the construction of a Saccharomyces cerevisiae platform strain for high-level production of very-long-chain fatty acid (VLCFA)-derived chemicals. Through rewiring the native fatty acid elongation system and implementing a heterologous Mycobacteria FAS I system, we establish an increased biosynthesis of VLCFAs in S. cerevisiae. VLCFAs can be selectively modified towards the fatty alcohol docosanol (C22H46O) by expressing a specific fatty acid reductase. Expression of this enzyme is shown to impair cell growth due to consumption of VLCFA-CoAs. We therefore implement a dynamic control strategy for separating cell growth from docosanol production. We successfully establish high-level and selective docosanol production of 83.5 mg l−1 in yeast. This approach will provide a universal strategy towards the production of similar high value chemicals in a more scalable, stable and sustainable manner.


Author(s):  
J. J. Bozzola ◽  
R. J. Mehta

Aculeacin A1 and papulacandin B2 are closely related antimycotic agents that interfere with the synthesis of alkalai-insoluble β 1-3 glucan in the cell wall of Candida albicans, Saccharomyces cerevisiae and Geotrichum lactis. The chemical structures of both agents contain a long-chain fatty acid, and both agents are strongly inhibitory to C. albicans and some other fungi while having negligible activity against bacteria or protozoa. Earlier studies involving light microscopy of aculeacin A treated cells revealed rounded, distorted cells aggregated in clumps. The sole TEM micrograph of aculeacin A treated cells showed invaginations and globular bodies associated with plasma membranes.


2005 ◽  
Vol 16 (1) ◽  
pp. 24-31 ◽  
Author(s):  
Jürgen Pohl ◽  
Axel Ring ◽  
Ümine Korkmaz ◽  
Robert Ehehalt ◽  
Wolfgang Stremmel

We previously reported that lipid rafts are involved in long-chain fatty acid (LCFA) uptake in 3T3-L1 adipocytes. The present data show that LCFA uptake does not depend on caveolae endocytosis because expression of a dominant negative mutant of dynamin had no effect on uptake of [3H]oleic acid, whereas it effectively prevented endocytosis of cholera toxin. Isolation of detergent-resistant membranes (DRMs) from 3T3-L1 cell homogenates revealed that FAT/CD36 was expressed in both DRMs and detergent-soluble membranes (DSMs), whereas FATP1 and FATP4 were present only in DSMs but not DRMs. Disruption of lipid rafts by cyclodextrin and specific inhibition of FAT/CD36 by sulfo-N-succinimidyl oleate (SSO) significantly decreased uptake of [3H]oleic acid, but simultaneous treatment had no additional or synergistic effects, suggesting that both treatments target the same mechanism. Indeed, subcellular fractionation demonstrated that plasma membrane fatty acid translocase (FAT/CD36) is exclusively located in lipid rafts, whereas intracellular FAT/CD36 cofractionated with DSMs. Binding assays confirmed that [3H]SSO predominantly binds to FAT/CD36 within plasma membrane DRMs. In conclusion, our data strongly suggest that FAT/CD36 mediates raft-dependent LCFA uptake. Plasma membrane lipid rafts might control LCFA uptake by regulating surface availability of FAT/CD36.


1970 ◽  
Vol 118 (2) ◽  
pp. 241-246 ◽  
Author(s):  
P. V. Subbaiah ◽  
P. S. Sastry ◽  
J. Ganguly

1. The presence of an active acyl-CoA–lysolecithin (1-acylglycerophosphorylcholine) acyltransferase was demonstrated in rat intestinal mucosa. 2. ATP and CoA were necessary for the incorporation of free [1-14C]oleic acid into lecithin (phosphatidylcholine). 3. The reaction was about 20 times as fast with [1-14C]oleoyl-CoA as with free oleic acid, CoA and ATP. 4. With 1-acylglycerophosphorylcholine as the acceptor, both oleic acid and palmitic acid were incorporated into the β-position of lecithin; the incorporation of palmitic acid was 60% of that of oleic acid. 5. Of the various analogues of lysolecithin tested as acyl acceptors from [1-14C]oleoyl CoA, a lysolecithin with a long-chain fatty acid at the 1-position was most efficient. 6. The enzyme was mostly present in the brush-border-free particulate fraction of the intestinal mucosa. 7. Of the various tissues of rats tested for the activity, intestinal mucosa was found to be the most active, with testes, liver, kidneys and spleen following it in decreasing order.


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