The regulation and function of inositol phosphorylceramide synthase in the yeast Saccharomyces cerevisiae

TL;DRAbstract

IPC Synthase has been shown to be an essential membrane bound enzyme in yeast that catalyzes the transfer of PI to ceramide to yield the primary sphingolipid found in yeast, Inositolphosphorylceramide. A biochemical approach was taken to investigate the biological factors that regulate IC synthase activity in order to better understand the sphingolipid synthesis. A highly purified IPC synthase was purified over 1000-fold from the yeast Saccharomyces cerevisiae by a procedure that included Triton X-100 solubilization, as well as a series of ion exchange and hydrophobic column chromatography steps. The highly purified enzyme fraction contained three major bands at 45, 58 and 90 kDa. The 45 kDa band has been identified as the AUR1 gene that encodes for IPC synthase activity. The level of IPC synthase was shown to be regulated by the growth phase of the yeast cell. Enzyme activity and protein levels of IPC synthase were expressed at the highest levels during early and mid exponential phase

Chat with Paper

AI Agents for this Paper