ERG25/YGR060W Summary Help

Standard Name ERG25
Systematic Name YGR060W
Feature Type ORF, Verified
Description C-4 methyl sterol oxidase; catalyzes the first of three steps required to remove two C-4 methyl groups from an intermediate in ergosterol biosynthesis; mutants accumulate the sterol intermediate 4,4-dimethylzymosterol (1, 2, 3, 4 and see Summary Paragraph)
Name Description ERGosterol biosynthesis
Chromosomal Location
ChrVII:610564 to 611493 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All ERG25 GO evidence and references
  View Computational GO annotations for ERG25
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 12 genes
Resources
Pathways
Classical genetics
null
overexpression
repressible
Large-scale survey
null
reduction of function
repressible
Resources
337 total interaction(s) for 235 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 7
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 3
  • PCA: 85
  • Two-hybrid: 3

Genetic Interactions
  • Dosage Rescue: 2
  • Negative Genetic: 192
  • Positive Genetic: 39
  • Synthetic Growth Defect: 1
  • Synthetic Rescue: 3

Resources
Expression Summary
histogram
Resources
Length (a.a.) 309
Molecular Weight (Da) 36,479
Isoelectric Point (pI) 8.14
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrVII:610564 to 611493 | ORF Map | GBrowse
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..930 610564..611493 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000003292
SUMMARY PARAGRAPH for ERG25

ERG25 encodes C-4 methyl sterol oxidase, which catalyzes the first of three steps required to remove two C-4 methyl groups from an intermediate in ergosterol biosynthesis (3, 4, 1, 2). Cells lacking ERG25 are auxotrophic for ergosterol, and accumulate a methylated sterol interm ediate, 4,4-dimethylzymosterol (3). A combination of mutations in ERG11, which encodes lanosterol 14-alpha-demethylase, and mutations that reduce cellular heme levels (in HEM2 or HEM4) can suppress the erg25 null sterol auxotrophy (5). The hem2 and hem4 mutations also suppress the erg25 phenotype in the presence of an azole antifungal drug (5). Expression of the Candida albicans ERG25 homolog complements the S. cerevisiae erg25 null phenotype (6); a human homolog has also been cloned (7).

Last updated: 2005-06-29 Contact SGD

References cited on this page View Complete Literature Guide for ERG25
1) Lees ND, et al.  (1995) Cloning of the late genes in the ergosterol biosynthetic pathway of Saccharomyces cerevisiae--a review. Lipids 30(3):221-6
2) Parks LW, et al.  (1995) Biochemical and physiological effects of sterol alterations in yeast--a review. Lipids 30(3):227-30
3) Bard M, et al.  (1996) Cloning and characterization of ERG25, the Saccharomyces cerevisiae gene encoding C-4 sterol methyl oxidase. Proc Natl Acad Sci U S A 93(1):186-90
4) Paltauf F, et al.  (1992) "Regulation and compartmentalization of lipid synthesis in yeast." Pp. 415-500 in The Molecular and Cellular Biology of the Yeast Saccharomyces: Gene Expression, edited by Jones EW, Pringle JR and Broach JR. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
5) Gachotte D, et al.  (1997) A yeast sterol auxotroph (erg25) is rescued by addition of azole antifungals and reduced levels of heme. Proc Natl Acad Sci U S A 94(21):11173-8
6) Kennedy MA, et al.  (2000) Cloning and sequencing of the Candida albicans C-4 sterol methyl oxidase gene (ERG25) and expression of an ERG25 conditional lethal mutation in Saccharomyces cerevisiae. Lipids 35(3):257-62
7) Li L and Kaplan J  (1996) Characterization of yeast methyl sterol oxidase (ERG25) and identification of a human homologue. J Biol Chem 271(28):16927-33