Abstract:
:The yeast ERG4 gene encodes sterol C-24(28) reductase which catalyzes the final step in the biosynthesis of ergosterol. Deletion of ERG4 resulted in a complete lack of ergosterol and accumulation of the precursor ergosta-5,7,22,24(28)-tetraen-3beta-ol. An erg4 mutant strain exhibited pleiotropic defects such as hypersensitivity to divalent cations and a number of drugs such as cycloheximide, miconazole, 4-nitroquinoline, fluconazole, and sodium dodecyl sulfate. Similar to erg6 mutants, erg4 mutants are sensitive to the Golgi-destabilizing drug brefeldin A. Enzyme activity measurements with isolated subcellular fractions revealed that Erg4p is localized to the endoplasmic reticulum. This view was confirmed in vivo by fluorescence microscopy of a strain expressing a functional fusion of Erg4p to enhanced green fluorescent protein. We conclude that ergosterol biosynthesis is completed in the endoplasmic reticulum, and the final product is supplied from there to its membranous destinations.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Zweytick D,Hrastnik C,Kohlwein SD,Daum Gdoi
10.1016/s0014-5793(00)01290-4keywords:
subject
Has Abstractpub_date
2000-03-17 00:00:00pages
83-7issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(00)01290-4journal_volume
470pub_type
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