A Novel Cold-Sensitive Allele of the Rate-Limiting Enzyme of Fatty Acid Synthesis, Acetyl Coenzyme A Carboxylase, Affects the Morphology of the Yeast Vacuole through Acylation of Vac8p

Schneiter, Roger; Guerra, Cesar E.; Lampl, Manfred; Tatzer, Verena; Zellnig, Günther; Klein, Hannah L.; Kohlwein, Sepp D.

doi:10.1128/mcb.20.9.2984-2995.2000

Cited by 38 publications

(38 citation statements)

References 58 publications

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“…To determine whether inactivation of Acc1 correlates with suppression of the inositol auxotrophy of the snf1⌬ mutant, we employed soraphen A, a potent inhibitor of Acc1 activity (78). Cells with elevated Acc1 activity are more resistant to this compound than wild-type cells, while cells with lowered Acc1 activity are more sensitive (64,65). Relative to a wild-type strain, a snf1⌬ strain was significantly more resistant to soraphen A, suggesting an increase in Acc1 activity in the mutant strain (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…viously described acc1 mutants (65,66), exhibited an increased proportion of 16 carbon fatty acids, whether or not the snf1 mutation was also present. Thus, there was no clear correlation between the cellular fatty acid composition and the ability to express INO1 in the snf1 genetic background, which, however, does not exclude potential effects of specifically localized altered lipid species.…”

Section: Discussionmentioning

confidence: 99%

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Inhibition of Acetyl Coenzyme A Carboxylase Activity Restores Expression of the INO1 Gene in a snf1Mutant Strain of Saccharomyces cerevisiae

Shirra

Patton‐Vogt

Ulrich

et al. 2001

Molecular and Cellular Biology

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102

106

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Mutations in the Saccharomyces cerevisiae SNF1 gene affect a number of cellular processes, including the expression of genes involved in carbon source utilization and phospholipid biosynthesis. To identify targets of the Snf1 kinase that modulate expression of INO1, a gene required for an early, rate-limiting step in phospholipid biosynthesis, we performed a genetic selection for suppressors of the inositol auxotrophy of snf1⌬ strains. We identified mutations in ACC1 and FAS1, two genes important for fatty acid biosynthesis in yeast; ACC1 encodes acetyl coenzyme A carboxylase (Acc1), and FAS1 encodes the ␤ subunit of fatty acid synthase. Acc1 was shown previously to be phosphorylated and inactivated by Snf1. Here we show that snf1⌬ strains with increased Acc1 activity exhibit decreased INO1 transcription. Strains carrying the ACC1 suppressor mutation have reduced Acc1 activity in vitro and in vivo, as revealed by enzymatic assays and increased sensitivity to the Acc1-specific inhibitor soraphen A. Moreover, a reduction in Acc1 activity, caused by addition of soraphen A, provision of exogenous fatty acid, or conditional expression of ACC1, suppresses the inositol auxotrophy of snf1⌬ strains. Together, these findings indicate that the inositol auxotrophy of snf1⌬ strains arises in part from elevated Acc1 activity and that a reduction in this activity restores INO1 expression in these strains. These results reveal a Snf1-dependent connection between fatty acid production and phospholipid biosynthesis, identify Acc1 as a Snf1 target important for INO1 transcription, and suggest models in which metabolites that are generated or utilized during fatty acid biosynthesis can significantly influence gene expression in yeast.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Inhibition of Acetyl Coenzyme A Carboxylase Activity Restores Expression of the INO1 Gene in a snf1Mutant Strain of Saccharomyces cerevisiae

Shirra

Patton‐Vogt

Ulrich

et al. 2001

Molecular and Cellular Biology

Self Cite

102

106

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“…Acetyl coenzyme A carboxylase, the first enzyme in the FA synthesis pathway, is a rate-limiting enzyme for FA synthesis (Majerus and Kilburn, 1969). The recognition of the essential metabolic role of the enzyme in FA biosynthesis prompted numerous investigations into acetyl-CoA carboxylases from different sources (Schneiter et al, 2000;Rosa et al, 2003;Zhang et al, 2003). Malic enzyme is a cytoplasmic protein (L-malate-NADP 1 oxidoreductase) (decarboxylating), which catalyzes the oxidative decarboxylation of malate to pyruvate and CO 2 , simultaneously generating NADPH from NADP 1 .…”

Section: Discussionmentioning

confidence: 99%

Microarray analysis of genes differentially expressed in the liver of lean and fat chickens

Wang

Zhang

et al. 2010

Animal

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Excessive accumulation of lipids in the adipose tissue is one of the main problems faced by the broiler industry nowadays. In chicken, lipogenesis occurs essentially in the liver, in which much of the triglycerides that accumulate in avian adipose tissue are synthesized. In order to better understand the gene expression and its regulation in chicken liver, the gene expression profiles of liver at developmental stages of chicken (1 week, 4 weeks and 7 weeks of age) were investigated and differentially expressed genes between lean and fat chicken lines divergently selected for abdominal fat content for eight generations were screened. Our data indicated that 4 weeks of age was a very important stage on chicken liver lipogenesis compared to 1 week and 7 weeks of age, and the glycometabolism in chicken liver could be related to lipid metabolism and the difference of glycometabolism could be another potential reason for the fat and lean phenotype occurrence besides the difference of lipogenesis in chicken liver. Our result have established groundwork for further study of the basic genetic control of chicken obesity and will benefit chicken research communities as well as researches that use chicken as a model organism for developmental biology and human therapeutics.

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“…If the synthesis of Palmitoyl-CoA is impaired, vacuoles fragment, most likely due to inefficient Vac8 palmitoylation. 196 Furthermore, mutants depleted of the Palmitoyl-CoA binding protein Acb1 also display altered vacuole morphology, 166,197 although the primary effect caused by loss of Acb1 may be impaired sphingolipid biosynthesis. In sum, the data strongly argue for an active role of lipids in vacuole fusion.…”

Section: Lipid Requirementsmentioning

confidence: 99%

Yeast vacuole fusion: A model system for eukaryotic endomembrane dynamics

Ostrowicz¹,

Meiringer²,

Ungermann³

2008

Autophagy

102

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Vesicular transport in eukaryotic cells is concluded with the consumption of the vesicle at the target membrane. This fusion process relies on Rabs, tethers and SNAREs. Powerful in vitro fusion systems using isolated organelles were crucial to obtain insights into the underlying mechanism of membrane fusionfrom the initiation of fusion to lipid bilayer mixing. Among these systems, yeast vacuoles turned out to be particularly useful as they can be manipulated biochemically and genetically. Studies relying on this organelle have revealed insights into the connection of vacuole fusion to endomembrane biogenesis. A number of fusion factors were identified and characterized over the last several years, and placed into the fusion cascade. Within this review, we will present and discuss the current state of our knowledge on vacuole fusion.

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A Novel Cold-Sensitive Allele of the Rate-Limiting Enzyme of Fatty Acid Synthesis, Acetyl Coenzyme A Carboxylase, Affects the Morphology of the Yeast Vacuole through Acylation of Vac8p

Cited by 38 publications

References 58 publications

Inhibition of Acetyl Coenzyme A Carboxylase Activity Restores Expression of the INO1 Gene in a snf1Mutant Strain of Saccharomyces cerevisiae

Inhibition of Acetyl Coenzyme A Carboxylase Activity Restores Expression of the INO1 Gene in a snf1Mutant Strain of Saccharomyces cerevisiae

Microarray analysis of genes differentially expressed in the liver of lean and fat chickens

Yeast vacuole fusion: A model system for eukaryotic endomembrane dynamics

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