truncated RoDH-4 that lacks the first thirteen amino acids of the N-terminal segment is partially active and exhibits the apparent Km value for androsterone similar to that of the wild-type enzyme, truncated mutant behaves as an integral membrane protein
RDH1 mutant, deleting the positive charges from the C-terminal end of the leader, and inserting two arginine residues near the N-terminus of the signaling sequence causes 95% inversion from cytoplasmic to luminal, the mutant faces the lumen
protein that lacked all four hydrophobic segments remains associated with the membrane. Thus, the N-terminal and the C-terminal ends are both important for RoDH-4 activity and the removal of the putative transmembrane segments does not convert RoDH-4 into a soluble protein, suggesting additional sites of membrane interaction
RDH8 genotping and phenotyping in Han Chinese population, identification of single nucleotide polymorphisms in RDH8 gene: RDH855b (-1715G/A; rs3760753), RDH851 (-472C/T; rs2233789), and RDH8E5a (7826T/C; rs1644731), overview
mutants lacking amino-terminal 18 or 30 amino acids do not localize to endoplasmic reticulum but to mitochondria instead. Deletion mutant lacking 28 C-terminal amino acids localizes both to microsomal and mitochondrial fractions. Deletion of both 18 N-terminal and 28 C-terminal amino acids leeds to overwhelming detection in mitochondria. Fusion of N-terminal 22 amino acids of enzyme with green fluorescent protein localizes in endoplasmic reticulum. Fusion of N-terminal 18 amino acids of enzyme with green fluorescent protein shows diffuse localization. Fusion of green fluorescent protein with C-terminal 29 amino acids of enzyme shows diffuse cytoplasmic and nuclear localization.