| Autor: |
Dunn, Teresa M., Haak, Dale, Monaghan, Erin, Beeler, Troy J. |
| Zdroj: |
Yeast; March 1998, Vol. 14 Issue: 4 p311-321, 11p |
| Abstrakt: |
Saccharomyces cerevisiaemutants lacking Scs7p fail to accumulate the inositolphosphorylceramide (IPC) species, IPC‐C, which is the predominant form found in wild‐type cells. Instead scs7mutants accumulate an IPC‐B species believed to be unhydroxylated on the amide‐linked C26‐fatty acid. Elimination of the SCS7gene suppresses the Ca2+‐sensitive phenotype of csg1and csg2mutants. The CSG1and CSG2genes are required for mannosylation of IPC‐C and accumulation of IPC‐C by the csgmutants renders them Ca2+‐sensitive. The SCS7gene 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. Scs7p is therefore likely to be the enzyme that hydroxylates the C26‐fatty acid of IPC‐C. © 1998 John Wiley & Sons, Ltd. |
| Databáze: |
Supplemental Index |
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