Disease relevance of SCS7

• Expression of the S. cerevisiae FAH1 cytochrome b5 domain in Escherichia coli produces a soluble protein that exhibits the typical oxidized versus reduced differential absorbance spectra of cytochrome b5 [1].

High impact information on SCS7

• The results from additional genetic studies using the sphingolipid hydroxylase and copper transporter genes, SCS7 and CCC2, respectively, suggest a second possible point of sterol regulation at the level of complex sphingolipid hydroxylation [2].
• A search of the Saccharomyces cerevisiae genome data base for cytochrome b5-like sequences identified a 1.152-kilobase pair open reading frame, located on chromosome XIII at locus YMR272C (FAH1) [1].
• Disruption of the FAH1 gene in S. cerevisiae did not give any visible phenotype, and there was no observable difference in content or distribution of the most abundant long chain saturated and unsaturated 14-18-carbon fatty acid species [1].
• A yeast strain that lacks the FAH1 gene was resistant to syringomycin E, and failed to complement BW7 [3].
• Mutants of SCS7, a lipid hydroxylase, and SLC1, a putative acyl transferase with unknown substrate specificity, were profiled for their phospholipid and sphingolipid content [4].

Biological context of SCS7

• Elimination of the SCS7 gene suppresses the Ca(2+)-sensitive phenotype of csg1 and csg2 mutants [5].
• The SCS7 gene encodes a protein that contains both a cytochrome b5-like domain and a domain that resembles the family of cytochrome b5-dependent enzymes that use iron and oxygen to catalyse desaturation or hydroxylation of fatty acids and sterols [5].

References