High impact information on ERG10

• Specifically, the discovery of sterol-mediated feedback control of ERG10 transcription is reported [1].
• Deletion analysis of the ERG10 promoter region identified sequences involved in the expression of ERG10 [1].
• We found that AMY2 is linked to cly2, and both are on chromosome II. tsm0115 is on the left arm of chromosome XVI [2].
• Two recessive alleles of ERG10 and three temperature-sensitive recessive alleles of HMG1 (3-hydroxy-3-methyl-glutaryl-CoA reductase isoenzyme 1) were isolated in a screen for mevalonate auxotrophs in Saccharomyces cerevisiae [3].
• The essential, single-copy ERG10 gene was cloned by complementation of the temperature-sensitive phenotype of erg10-21 [3].

Biological context of ERG10

• Additionally, similar ERG10 and TRR1 gene expression patterns over the initial 24-h fermentation period highlighted a possible interaction between ergosterol biosynthesis and the oxidative stress response [4].
• Consistent with this, cells of an erg10 mutant strain showed a clear phenotype of cold and freeze sensitivity [5].
• This identity included the active site cysteines located at amino acids 91 and 384 in the Erg10 protein [3].
• Two genes encoding acetoacetyl-CoA thiolase (thiolase I; EC 2.3.1.9), whose localization in peroxisomes was first found with an n-alkane-utilizing yeast, Candida tropicalis, were isolated from the lambda EMBL3 genomic DNA library prepared from the yeast genomic DNA [6].
• Isolation and characterization of acetoacetyl-CoA thiolase gene essential for n-decane assimilation in yeast Yarrowia lipolytica [7].

Anatomical context of ERG10

• These facts suggest that the complete degradation of fatty acids to acetyl-CoA is carried out in yeast peroxisomes by the cooperative contribution of acetoacetyl-CoA thiolase and 3-ketoacyl-CoA thiolase [8].
• The presence of two types of thiolases, acetoacetyl-CoA thiolase and 3-ketoacyl-CoA thiolase, was demonstrated in peroxisomes of n-alkane-grown Candida tropicalis [Kurihara, T., Ueda, M., & Tanaka, A. (1989) J. Biochem. 106, 474-478], while acetoacetyl-CoA thiolase was also shown to be present in cytosol [9].

Associations of ERG10 with chemical compounds

• The first step in ergosterol biosynthesis in Saccharomyces cerevisiae consists of the condensation of two acetyl coenzyme A (acetyl-CoA) moieties by acetoacetyl-CoA thiolase, encoded by ERG10 [10].
• Growth of mutants impaired in acetoacetyl-CoA thiolase cannot be recovered by mevalonic acid supplementation, suggesting a role of acetoacetyl-CoA or thiolase not linked to sterol pathway [11].
• The homozygous ct-t1a delta/t1bdelta null mutation abolished the activity of acetoacetyl-CoA thiolase and resulted in mevalonate auxotrophy [12].
• From the results of hybridization of DNA probes of yeast peroxisomal enzymes--catalase, acyl-CoA oxidase, carnitine acetyltransferase, isocitrate lyase, malate synthase, acetoacetyl-CoA thiolase, and 3-ketoacyl-CoA thiolase--to Southern transfers of CHEF gels, these genes were proven not necessarily to be located on the same chromosome [13].
• Of the enzymes involved in cholesterol synthesis, two enzymes, acetoacetyl-CoA thiolase (EC 2.3.1.9) and 3-hydroxy-3-methylglutaryl-CoA reductase (EC 1.1.1.34), were specifically inhibited by the antibiotic [14].

Other interactions of ERG10

• The mRNA level of TPI1 and ERG10 genes was higher in freeze-stressed than in control samples of the tolerant strain [5].
• A 5-10-fold decrease is observed for acetoacetyl-CoA thiolase and HMG-CoA synthase [15].
• These results indicate that PAT1 encodes peroxisomal acetoacetyl-CoA thiolase and is essential for n-decane utilization in Y. lipolytica [7].

Analytical, diagnostic and therapeutic context of ERG10

• Northern blot and sequence analysis indicate that the ERG10 gene is highly expressed, and biochemical and genetic evidence show that it encodes the cytoplasmic acetoacetyl CoA thiolase [16].
• We reported that immunoelectron microscopy was an excellent tool for determining the subcellular localization of thiolase isozymes, acetoacetyl-CoA thiolase (T-I) and 3-ketoacyl-CoA thiolase (T-III) in n-alkane-grown Candida tropicalis cells (KAMASAWA, N. et al., (1992). Cell Struct. Funct., 17: 203-207) [17].
• Acetoacetyl-CoA thiolase (Thiolase I) and 3-ketoacyl-CoA thiolase (Thiolase III) found in peroxisomes of an n-alkane-utilizing yeast, Candida tropicalis pK 233, were each purified to homogeneity by successive column chromatographies [18].

References