ERG10 from Saccharomyces cerevisiae encodes acetoacetyl-CoA thiolase.

Hiser, Laree; Basson, M E; Rine, Jasper

doi:10.1016/s0021-9258(18)31705-8

Cited by 52 publications

(18 citation statements)

References 32 publications

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“…A. fumigatus cytosolic ACAT is homologous to S. cerevisiae cytosolic ACAT (NCBI accession: NP_015297.1), the product of the ERG10 gene (NCBI Gene ID: 856079). 46 Intriguingly, in comparison to ACATs from higher eukaryotes, cytosolic ACATs from plant and fungi are more similar in terms of amino acid sequence to mitochondrial ACATs than to cytosolic ACATs. The crystal structure of human mitochondrial ACAT (hT2) revealed a K + binding site that stabilizes the substrate binding pocket and the catalytic histidine, providing a structural basis for its activation by K + ions.…”

Section: ■ Resultsmentioning

confidence: 99%

“…In fungi, S. cerevisiae cytosolic ACAT is the product of a single gene, ERG10, and is essential for viability in the absence of exogenous mevalonate. 46 Similarly, Candida tropicalis cytosolic ACAT null mutant is auxotrophic for mevalonate. 20 Unsurprisingly, ERG10 has also been shown to be essential for growth in A. fumigatus, 47 presenting cytosolic ACAT as a potential target for novel antifungals.…”

Section: ■ Introductionmentioning

confidence: 99%

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Structure of Aspergillus fumigatus Cytosolic Thiolase: Trapped Tetrahedral Reaction Intermediates and Activation by Monovalent Cations

2018

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The new agreement specifically addresses what authors can do with different versions of their manuscripte.g. use in theses and collections, teaching and training, conference presentations, sharing with colleagues, and posting on websites and repositories. The terms under which these uses can occur are clearly identified to prevent misunderstandings that could jeopardize final publication of a manuscript (Section II, Permitted Uses by Authors).

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Section: ■ Resultsmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

Structure of Aspergillus fumigatus Cytosolic Thiolase: Trapped Tetrahedral Reaction Intermediates and Activation by Monovalent Cations

2018

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“…Recognizable PTS were absent in the sequences of both R. sativus and the second copy of A. thaliana. The yeast erg10 gene codes for a cytosolic thiolase II, with a well-characterized function in the biosynthesis of ergosterol (Hiser et al 1994) and clustered with other fungal sequences (Fig. 1).…”

Section: Diversity Of Biochemical Functions Subcellular Localization and Phylogenetic Distribution Of Thiolasesmentioning

confidence: 98%

Phylogenetic Analysis of Eukaryotic Thiolases Suggests Multiple Proteobacterial Origins

2005

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Eukaryotic thiolases are essential enzymes located in three different compartments (peroxisome, mitochondrion, and cytosol) that can display catabolic or anabolic functions. They are responsible for the thiolytic cleavage of oxidized acyl-CoA (thiolase I; EC 2.3.1.16) and the synthesis or degradation of acetoacetyl-CoA (thiolase II; EC 2.3.1.9). Phylogenetic analysis of eukaryotic thiolase sequences showed that they form six distinct clusters, one of them highly divergent, which are in good correlation with their class and subcellular location. When analyzed together with a representative sample of prokaryotic thiolases, all eukaryotic thiolase groups emerged close to proteobacterial sequences. Metazoan cytosolic thiolase II was related to alpha-proteobacterial sequences, suggesting a mitochondrial origin. Unexpectedly, cytosolic thiolases from green plants and fungi as well as at least one member of all eukaryotic peroxisomal and mitochondrial thiolases had delta-proteobacteria as closest relatives. Our analysis suggests that these eukaryotic peroxisomal and mitochondrial thiolases may have been acquired from delta-proteobacteria prior to the ancestor of all known eukaryotes.

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“…Thiolase I, also known as Pot1, localizes in the peroxisome and is involved in β-oxidation of fatty acids, and the pot mutant is reported to be lethal in medium with oleic acid as the sole carbon source (11, 12). Thiolase II, also known as Erg10, localizes in the cytosol and is involved in the first step of ergosterol biosynthesis where it condenses two acetyl CoA molecules to acetoacetyl coenzyme A (13). Similar to S. cerevisiae , Xanthophyllomyces dendrorhous harbors two thiolases (Erg10 and Pot1); Erg10 is essential for ergosterol biosynthesis, while Pot1 is not essential for cell growth, although it indirectly affects pigment production (14).…”

Section: Introductionmentioning

confidence: 99%

Identification of Six Thiolases and their Effects on Fatty Acid and Ergosterol Biosynthesis in Aspergillus oryzae

Huang

Niu

Jin

et al. 2021

Preprint

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Thiolase plays important roles in lipid metabolism. It can be divided into degradative thiolases (Thioase I) and biosynthetic thiolases (thiolases II), which are involved in fatty acid β-oxidation and acetoacetyl-CoA biosynthesis, respectively. The Saccharomyces cerevisiae (S. cerevisiae) genome harbors only one gene each for thioase I and thiolase II, namely, Pot1 and Erg10, respectively. In this study, six thiolases (named AoErg10A−AoErg10F) were identified in Aspergillus oryzae (A. oryzae) genome using bioinformatics analysis. Quantitative reverse transcription–PCR (qRT-PCR) indicated that the expression of these six thiolases varied at different growth stages and under different forms of abiotic stress. Subcellular localization analysis showed that AoErg10A was located in the cytoplasm, AoErg10B and AoErg10C in the mitochondria, and AoErg10D-AoErg10F in the peroxisome. Yeast heterologous complementation assays revealed that AoErg10A, AoErg10D, AoErg10E, AoErg10F and cytoplasmic AoErg10B (AoErg10BΔMTS) recovered the phenotypes of S. cerevisiae erg10 weak and lethal mutants, and that only AoErg10D-F recovered the phenotype of the pot1 mutant that cannot use oleic acid as the carbon source. Overexpression of AoErg10s either affected the growth speed or sporulation of the transgenic strains. In addition, the fatty acid and ergosterol content changed in all the AoErg10-overexpressing strains. This study revealed the function of six thiolases in A. oryzae and their effect on growth, and fatty acid and ergosterol biosynthesis, which may lay the foundation for genetic engineering for lipid metabolism in A. oryzae or other fungi.ImportanceThiolase including thioase I and thiolase II, plays important roles in lipid metabolism. A. oryzae, one of the most industrially important filamentous fungi, has been widely used for manufacturing oriental fermented food such as sauce, miso, and sake for a long time. Besides, A. oryzae has a high capability in production of high lipid content and has been used for lipid production. Thus, it is very important to investiagte the function of thiolases in A. oryzae. In this study, six thiolase (named AoErg10A-AoErg10F) were identified by bioinformatics analysis. Unlike other reported thiolases in fungi, three of the six thiolases showed dual function of thioase I and thiolase II in S. cerevisiae, indicating the lipid metabolism is more complex in A. oryzae. The reveal of founction of these thiolases in A. oryzae can lay the foundation for genetic engineering for lipid metabolism in A. oryzae or other fungi.

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ERG10 from Saccharomyces cerevisiae encodes acetoacetyl-CoA thiolase.

Cited by 52 publications

References 32 publications

Structure of Aspergillus fumigatus Cytosolic Thiolase: Trapped Tetrahedral Reaction Intermediates and Activation by Monovalent Cations

Structure of Aspergillus fumigatus Cytosolic Thiolase: Trapped Tetrahedral Reaction Intermediates and Activation by Monovalent Cations

Phylogenetic Analysis of Eukaryotic Thiolases Suggests Multiple Proteobacterial Origins

Identification of Six Thiolases and their Effects on Fatty Acid and Ergosterol Biosynthesis in Aspergillus oryzae

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