4. International Congress on Applied Biological Sciences (ICABS), Eskişehir, Turkey, 3 - 05 May 2018, vol.1, no.1, pp.1
The biosynthesis of trehalose is catalyzed by synthase enzyme complex and degraded by neutral trehalase enzyme. Yarrowia lipolytica is a dimorphic yeast that can shift from yeast to hyphal form and vice versa. Y. lipolytica is also used as a model organism for understanding of lipid metabolism in higher eukaryotes. YlTPS1 and YlNTH1 genes are responsible from the recycling of threhalose in Y. lipolytica. The aim of this work is to determine the expression patterns of YlTPS1 and YlNTH1 genes under different carbon sources by using RNAseq study. The files used in this analysis were obtained from the EMBL-EBI data bank and Study ID is “PRJEB2863”. The substrates used in the work are Alkane, Glucose, Glycerol, Oleic Acid, Tributyrin and Triolein. The run accession numbers of substrates are ERR073010, ERR073011, ERR073009, ERR073008, ERR073012 and ERR073007, respectively. "Trimmomatic" tool was used for croping the readings in the next generation sequencing files. Reference genome of Y. lipolytica were obtained from Ensembl genome data base. The files were converted to “ERR0730xx_tophat2.bam” files and used in the "FeatureCounts" tool. We found that 176, 185, 155, 306, 141 and 158 read counts were detected for YlNTH1 gene, and 360, 479, 480, 557, 559 and 525 read counts detected for YlTPS1 gene in alkane, glucose, glycerol, oleic acid, tributyrin and triolein carbon sources, respectively. The transcript level YlTPS1 gene was 2 to 4 times higher than YlNTH1 gene. In Y. lipolytica the rate of trehalose synthesis is greater than rate of breakdown in different carbon sources.