Cloning and functional characterization of a fatty acid synthase component FAS2 gene from Saccharomyces kluyveri

Abstract

A gene coding the alpha subunit of fatty acid synthase (FAS2) was isolated from the budding yeast Saccharomyces kluyveri. Nucleotide sequence analysis indicated that this gene, termed Sk-FAS2, coded a protein having an amino acid sequence 83% identical to the FAS2 protein of S. cerevisiae (Sc-FAS2). The Sk-FAS2 gene was able to functionally complement an S. cerevisiae fas2 disruptant. This Sk-FAS2-expressing strain was found to produce larger amounts of C18 than C16, in contrast to the Sc-FAS2-expressing fas2 strain. In addition, fusion genes of Sk-FAS2 and Sc-FAS2 were transformed into a fas2-disrupted strain of S. cerevisiae, and fatty acid analysis of these transformants suggested that the region containing the acyl carrier protein and beta-ketoacyl reductase domains of yeast FAS2 protein play an important role in determining carbon chain length of fatty acids.

Substrate Specificity and Regioselectivity of Δ12 and ω3 Fatty Acid Desaturases fromSaccharomyces kluyveri

“…The lipids were then methylated with 1% sulfuric acid in methanol at 90 C for 2 h, as described previously. 21) The resulting fatty acid methyl esters (FAMEs) were extracted with hexane. The FAMEs were analyzed by gas-liquid chromatography (GLC: GC-18A, Shimadzu, Kyoto, Japan) with a 0:25 mm  25 m HR-SS-10 capillary column (Shinwa Chemical Industries, Kyoto, Japan).…”

Krüppel-homologue 1regulates the development ofTuta absolutaand its cascade regulation pattern in the juvenile hormone signalling pathway

“…JHAMT plays a role in the last step of the insect JH biosynthesis pathway, during which it can activate and convert JH acid and inactive JH precursor into active JH [ 51 ]. Fatty acid synthase (FAS) catalyses the synthesis of acetyl-CoA, malonyl-CoA and NADPH into long-chain saturated Fatty acids [ 52 , 53 ], thereby regulating lipid accumulation during diapause in insects [ 54 ]. Vitellogenin (Vg) is a precursor protein of vitelloprotein, which provides energy reserves for embryonic development [ 55 , 56 ].…”