truncation of amphipathic helices within the N- and C-terminal domains of isoform Atf1 (residues 24-41 and 508-525) impair endoplasmic reticulum localization and membrane association. Mutations of the basic or hydrophobic residues in the N-terminal helix and hydrophobic residues in the C-terminal helix of Atf1 disrupt ER association and subsequent sorting from the ER to lipid droplets. Similar amphipathic helices are found at both ends of isoform Atf2, enabling ER and lipid droplet association. Mutations to the N- and C-terminal helices of Atf2 prevent membrane association
reconstruction of the engineered pathways for production of indole-3-ethanol and indole-3-ethanol acetate from glucose in Escherichia coli strain MG1655, enzyme ATF1 is included catalyzing the formation of indole-3-ethanol acetate from indole-3-ethanol, pathway and method evaluation, overview
truncation of amphipathic helices within the N- and C-terminal domains of isoform Atf1 (residues 24-41 and 508-525) impair endoplasmic reticulum localization and membrane association. Mutations of the basic or hydrophobic residues in the N-terminal helix and hydrophobic residues in the C-terminal helix of Atf1 disrupt ER association and subsequent sorting from the ER to lipid droplets. Similar amphipathic helices are found at both ends of isoform Atf2, enabling ER and lipid droplet association. Mutations to the N- and C-terminal helices of Atf2 prevent membrane association
reconstruction of the engineered pathways for production of indole-3-ethanol and indole-3-ethanol acetate from glucose in Escherichia coli strain MG1655, enzyme ATF1 is included catalyzing the formation of indole-3-ethanol acetate from indole-3-ethanol, pathway and method evaluation, overview