Engineering membrane asymmetry to increase medium‐chain fatty acid tolerance in Saccharomyces cerevisiae

2021 ◽  
Author(s):  
Hui Liu ◽  
Weijia Yuan ◽  
Pei Zhou ◽  
Guangjie Liang ◽  
Cong Gao ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Fatty Acid ◽  
Acid Tolerance ◽  
Chain Fatty Acid ◽  
Medium Chain Fatty Acid ◽  
Membrane Asymmetry ◽  
Medium Chain

scholarly journals Pex11p Plays a Primary Role in Medium-Chain Fatty Acid Oxidation, a Process That Affects Peroxisome Number and Size in Saccharomyces cerevisiae

2000 ◽  
Vol 150 (3) ◽  
pp. 489-498 ◽  
Author(s):  
Carlo W.T. van Roermund ◽  
Henk F. Tabak ◽  
Marlene van den Berg ◽  
Ronald J.A. Wanders ◽  
Ewald H. Hettema
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Fatty Acid ◽  
Chain Fatty Acid ◽  
Medium Chain Fatty Acid ◽  
Acid Oxidation ◽  
Primary Role ◽  
Peroxisomal Membrane ◽  
Intact Cells ◽  
Medium Chain ◽  
Mutant Cells

The Saccharomyces cerevisiae peroxisomal membrane protein Pex11p has previously been implicated in peroxisome proliferation based on morphological observations of PEX11 mutant cells. Pex11p-deficient cells fail to increase peroxisome number in response to growth on fatty acids and instead accumulate a few giant peroxisomes. We report that mutants deficient in genes required for medium-chain fatty acid (MCFA) β-oxidation display the same phenotype as Pex11p-deficient cells. Upon closer inspection, we found that Pex11p is required for MCFA β-oxidation. Disruption of the PEX11 gene results in impaired formation of MCFA-CoA esters as measured in intact cells, whereas their formation is normal in cell lysates. The sole S. cerevisiae MCFA-CoA synthetase (Faa2p) remains properly localized to the inner leaflet of the peroxisomal membrane in PEX11 mutant cells. Therefore, the in vivo latency of MCFA activation observed in Pex11p-deficient cells suggests that Pex11p provides Faa2p with substrate. When PEX11 mutant cells are shifted from glucose to oleate-containing medium, we observed an immediate deficiency in β-oxidation of MCFAs whereas giant peroxisomes and a failure to increase peroxisome abundance only became apparent much later. Our observations suggest that the MCFA oxidation pathway regulates the level of a signaling molecule that modulates the number of peroxisomal structures in a cell.

scholarly journals Transcriptomic response of Saccharomyces cerevisiae to octanoic acid production

2021 ◽  
Vol 21 (2) ◽  
Author(s):  
Leonie Baumann ◽  
Tyler Doughty ◽  
Verena Siewers ◽  
Jens Nielsen ◽  
Eckhard Boles ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Fatty Acid ◽  
Acid Production ◽  
Octanoic Acid ◽  
Chain Fatty Acid ◽  
Medium Chain Fatty Acid ◽  
Cell Physiology ◽  
Transcriptomic Response ◽  
Promising Alternative ◽  
Medium Chain

ABSTRACT The medium-chain fatty acid octanoic acid is an important platform compound widely used in industry. The microbial production from sugars in Saccharomyces cerevisiae is a promising alternative to current non-sustainable production methods, however, titers need to be further increased. To achieve this, it is essential to have in-depth knowledge about the cell physiology during octanoic acid production. To this end, we collected the first RNA-Seq data of an octanoic acid producer strain at three time points during fermentation. The strain produced higher levels of octanoic acid and increased levels of fatty acids of other chain lengths (C6–C18) but showed decreased growth compared to the reference. Furthermore, we show that the here analyzed transcriptomic response to internally produced octanoic acid is notably distinct from a wild type's response to externally supplied octanoic acid as reported in previous publications. By comparing the transcriptomic response of different sampling times, we identified several genes that we subsequently overexpressed and knocked out, respectively. Hereby we identified RPL40B, to date unknown to play a role in fatty acid biosynthesis or medium-chain fatty acid tolerance. Overexpression of RPL40B led to an increase in octanoic acid titers by 40%.

scholarly journals The Saccharomyces cerevisiae EHT1 and EEB1 Genes Encode Novel Enzymes with Medium-chain Fatty Acid Ethyl Ester Synthesis and Hydrolysis Capacity

2006 ◽  
Vol 281 (7) ◽  
pp. 4446-4456 ◽  
Author(s):  
Sofie M.G. Saerens ◽  
Kevin J. Verstrepen ◽  
Stijn D.M. Van Laere ◽  
Arnout R.D. Voet ◽  
Patrick Van Dijck ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Fatty Acid ◽  
Ethyl Ester ◽  
Acid Ethyl Ester ◽  
Fatty Acid Ethyl Ester ◽  
Chain Fatty Acid ◽  
Medium Chain Fatty Acid ◽  
Ester Synthesis ◽  
Medium Chain

scholarly journals Discovery and identification of medium‐chain fatty acid responsive promoters in Saccharomyces cerevisiae

2020 ◽  
Vol 20 (5-6) ◽  
pp. 186-196
Author(s):  
Li Han ◽  
Danya Han ◽  
Lei Li ◽  
Shen Huang ◽  
Peixin He ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Fatty Acid ◽  
Chain Fatty Acid ◽  
Medium Chain Fatty Acid ◽  
Medium Chain

scholarly journals Identification of a Peroxisomal ATP Carrier Required for Medium-Chain Fatty Acid β-Oxidation and Normal Peroxisome Proliferation in Saccharomyces cerevisiae

2001 ◽  
Vol 21 (13) ◽  
pp. 4321-4329 ◽  
Author(s):  
Carlo W. T. van Roermund ◽  
Roy Drissen ◽  
Marlene van den Berg ◽  
Lodewijk Ijlst ◽  
Ewald H. Hettema ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Fatty Acid ◽  
Normal Growth ◽  
Chain Fatty Acid ◽  
Medium Chain Fatty Acid ◽  
Wild Type ◽  
Peroxisomal Membrane ◽  
Oxidation Activity ◽  
Medium Chain ◽  
Mutant Cells

ABSTRACT We have characterized the role of YPR128cp, the orthologue of human PMP34, in fatty acid metabolism and peroxisomal proliferation inSaccharomyces cerevisiae. YPR128cp belongs to the mitochondrial carrier family (MCF) of solute transporters and is localized in the peroxisomal membrane. Disruption of theYPR128c gene results in impaired growth of the yeast with the medium-chain fatty acid (MCFA) laurate as a single carbon source, whereas normal growth was observed with the long-chain fatty acid (LCFA) oleate. MCFA but not LCFA β-oxidation activity was markedly reduced in intact ypr128cΔ mutant cells compared to intact wild-type cells, but comparable activities were found in the corresponding lysates. These results imply that a transport step specific for MCFA β-oxidation is impaired in ypr128cΔ cells. Since MCFA β-oxidation in peroxisomes requires both ATP and CoASH for activation of the MCFAs into their corresponding coenzyme A esters, we studied whether YPR128cp is an ATP carrier. For this purpose we have used firefly luciferase targeted to peroxisomes to measure ATP consumption inside peroxisomes. We show that peroxisomal luciferase activity was strongly reduced in intact ypr128cΔ mutant cells compared to wild-type cells but comparable in lysates of both cell strains. We conclude that YPR128cp most likely mediates the transport of ATP across the peroxisomal membrane.

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