Phospholipid Biosynthesis in Yeast

Carman, George M.; Henry, Susan A.

doi:10.1146/annurev.bi.58.070189.003223

Cited by 321 publications

(285 citation statements)

References 2 publications

Supporting

Mentioning

277

Contrasting

Order By: Relevance

“…We analyzed the phospholipid components (PC, PI, PS, and PE) in both Me 2 SO-treated and non-treated cells from the mid-exponential to stationary phase to investigate possible differences in biosynthesis of these membrane components. If there was any defection or anomaly in gene expression in the phospholipid synthesis pathway, the relative proportions of phospholipid components, such as PC, PI, PS, and PE, should change (32). These studies demonstrated that the amounts of phospholipid increased greatly after 4 -6 h of Me 2 SO treatment (Fig.…”

Section: Me 2 So Concentration and Duration Of Exposure-s Cerevisiaementioning

confidence: 78%

“…SAM1 and SAM2 genes encode two distinct forms of AdoMet synthetase and catalyze the biosynthesis of AdoMet from methionine in the methionine synthesis pathway. In the biosynthetic pathway to PC, PE is methylated by PE methyltransferase (CHO2) and phospholipid methyltransferase (OPI3), which both utilize AdoMet as the methyl donor (32,33). AdoHcy resulting from the demethylation of AdoMet is converted to methionine or AdoMet in the methionine synthesis pathway (Fig.…”

Section: Me 2 So Concentration and Duration Of Exposure-s Cerevisiaementioning

confidence: 99%

“…In phospholipid biosynthesis (Fig. 4), AdoMet is needed in the last three methylation reactions and is transformed to AdoHcy by a demethylation reaction (32,33). AdoHcy is converted to homocysteine in the methionine biosynthesis pathway, which is then remethylated to methionine by methionine synthetase (MET17/25 and MET6).…”

Section: Me 2 So Concentration and Duration Of Exposure-s Cerevisiaementioning

confidence: 99%

“…In general, a number of genes involved in phospholipid biosynthesis are known to be repressed after addition of inositol and choline to the growth medium (inositol-choline regulation) (31,32). The regulatory responses to inositol and choline are established by specific regulatory regions, conventionally referred to as upstream activation sequence, and localized in their upstream region (47,48).…”

Section: Me 2 So Concentration and Duration Of Exposure-s Cerevisiaementioning

confidence: 99%

See 3 more Smart Citations

Dimethyl Sulfoxide Exposure Facilitates Phospholipid Biosynthesis and Cellular Membrane Proliferation in Yeast Cells

Murata¹,

Watanabe²,

Sato³

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

Me 2 SO is a polar solvent that is widely used in biochemistry, pharmacology, and industry. Although there are several reports in the literature concerning the biological effects of Me 2 SO, the total cellular response remains unclear. In this paper, DNA microarray technology combined with the hierarchical clustering bioinformatics tool was used to assess the effects of Me 2 SO on yeast cells. We found that yeast exposed to Me 2 SO increased phospholipid biosynthesis through up-regulated gene expression. It was confirmed by Northern blotting that the level of INO1 and OPI3 gene transcripts, encoding key enzymes in phospholipid biosynthesis, were significantly elevated following treatment with Me 2 SO. Furthermore, the phospholipid content of the cells increased during exposure to Me 2 SO as shown by conspicuous incorporation of a lipophilic fluorescent dye (3,3 -dihexyloxacarbocyanine iodide) into the cell membranes. From these results we propose that Me 2 SO treatment induces membrane proliferation in yeast cells to alleviate the adverse affects of this chemical on membrane integrity.Dimethyl sulfoxide (Me 2 SO) 1 is widely used as a solvent in the chemical industry and as a cryoprotectant in biotechnology. It is present in the environment as a waste product of the paper industry and from the production of dimethyl sulfide (DMS) and also arises from the degradation of sulfur-containing pesticides (1). In addition, Me 2 SO forms naturally from photooxidation of DMS in the atmosphere and from degradation of DMS by phytoplankton in the marine environment (2). Because Me 2 SO has low volatility and is highly hygroscopic, it is rapidly scavenged from the atmosphere by rain and returned to earth, and thereby plays a role in the global sulfur cycle (1, 3).Microorganisms, including both prokaryotes and eukaryotes, have the capability of reducing Me 2 SO and can utilize it as a terminal electron acceptor during anaerobic growth (4 -6). Me 2 SO reductase from Escherichia coli and Rhodobacter sphaeroides catalyzes the reduction of Me 2 SO to DMS (7-9). This enzyme, which contains a molybdenum cofactor at the active center, is well characterized at the biochemical, biophysical, and molecular level and provides an excellent model system for investigating the structure and mechanism of electron transfer chain complexes (1, 10). Saccharomyces cerevisiae has a number of NADPH-dependent enzymes that, in conjunction with methionine sulfoxide reductase (MXR1), can reduce Me 2 SO to DMS (11).In E. coli, the combination of divalent cations as Ca 2ϩ and Me 2 SO has been shown to stimulate the efficiency of DNA transfer into the cell (12). In the case of mammalian cells, it is reported that the transfection efficiency is increased by Me 2 SO treatment after electroporation (13). The exact mechanism of how Me 2 SO increases membrane permeability leading to DNA uptake is unclear.In mammalian cells Me 2 SO (2% (v/v)) can induce morphological changes, for example in mouse erythroleukemic cells (14), or cause differentiation, for example ...

show abstract

Section: Me 2 So Concentration and Duration Of Exposure-s Cerevisiaementioning

confidence: 78%

Section: Me 2 So Concentration and Duration Of Exposure-s Cerevisiaementioning

confidence: 99%

Section: Me 2 So Concentration and Duration Of Exposure-s Cerevisiaementioning

confidence: 99%

Section: Me 2 So Concentration and Duration Of Exposure-s Cerevisiaementioning

confidence: 99%

See 2 more Smart Citations

Dimethyl Sulfoxide Exposure Facilitates Phospholipid Biosynthesis and Cellular Membrane Proliferation in Yeast Cells

Murata¹,

Watanabe²,

Sato³

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…In the model eukaryote Saccharomyces cerevisiae, PC is synthesized by complementary pathways that are common to those found in mammalian cells 2 ( Fig. 1) (1,4,(13)(14)(15)(16)(17). In the CDP-DAG pathway, PC is synthesized from CDP-DAG via the reactions catalyzed by PS synthase (18 -20), PS decarboxylase (21-23), PE methyltransferase (24, 25), and phospholipid methyltransferase (24,26).…”

mentioning

confidence: 99%

Regulation of Phospholipid Synthesis in the Yeast cki1Δ eki1Δ Mutant Defective in the Kennedy Pathway

Choi

Sreenivas

Han

et al. 2004

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

In the yeast Saccharomyces cerevisiae, the most abundant phospholipid phosphatidylcholine is synthesized by the complementary CDP-diacylglycerol and Kennedy pathways. Using a cki1⌬ eki1⌬ mutant defective in choline kinase and ethanolamine kinase, we examined the consequences of a block in the Kennedy pathway on the regulation of phosphatidylcholine synthesis by the CDP-diacylglycerol pathway. The cki1⌬ eki1⌬ mutant exhibited increases in the synthesis of phosphatidylserine, phosphatidylethanolamine, and phosphatidylcholine via the CDP-diacylglycerol pathway. The increase in phospholipid synthesis correlated with increased activity levels of the CDPdiacylglycerol pathway enzymes phosphatidylserine synthase, phosphatidylserine decarboxylase, phosphatidylethanolamine methyltransferase, and phospholipid methyltransferase. However, other enzyme activities, including phosphatidylinositol synthase and phosphatidate phosphatase, were not affected in the cki1⌬ eki1⌬ mutant. For phosphatidylserine synthase, the enzyme catalyzing the committed step in the pathway, activity was regulated by increases in the levels of mRNA and protein. Decay analysis of CHO1 mRNA indicated that a dramatic increase in transcript stability was a major component responsible for the elevated level of phosphatidylserine synthase. These results revealed a novel mechanism that controls phospholipid synthesis in yeast.PC 1 is the most abundant phospholipid in the membranes of eukaryotic cells (1-4). It serves as a structural component of the membrane and as a source of bioactive lipids (e.g. lyso-PC, PA, DAG) (1-5). The importance of PC is underscored by the fact that alterations in its metabolism are linked to apoptosis (6 -9) and oncogenic transformation (10 -12). In the model eukaryote Saccharomyces cerevisiae, PC is synthesized by complementary pathways that are common to those found in mammalian cells 2 ( Fig. 1) (1,4,(13)(14)(15)(16)(17). In the CDP-DAG pathway, PC is synthesized from CDP-DAG via the reactions catalyzed by PS synthase (18 -20), PS decarboxylase (21-23), PE methyltransferase (24, 25), and phospholipid methyltransferase (24,26). In the CDP-choline branch of the Kennedy pathway, PC is synthesized from choline via the reactions catalyzed by choline kinase (27), phosphocholine cytidylyltransferase (28), and choline phosphotransferase (29,30). Analyses of mutations in S. cerevisiae (4, 31, 32), as well as in mammalian cells (33,34) indicate that the physiological role(s) of PC synthesized by the two pathways are different.The contribution of the CDP-DAG and Kennedy pathways for PC synthesis in wild type S. cerevisiae is dependent on the exogenous supply of choline (35). When grown in the presence of choline, yeast primarily synthesizes PC via the Kennedy pathway (35). On the other hand, when cells are grown in the absence of choline, PC is primarily synthesized via the CDP-DAG pathway (35). Yet, even under this growth condition, the Kennedy pathway still contributes to the synthesis of PC (36 -41). The choline required for the Kenne...

show abstract

Functional characterization of the repeated UASINO element in the promoters of the INO1 and CHO2 genes of yeast

Koipally

Ashburner

Bachhawat

et al. 1996

Yeast

Self Cite

View full text Add to dashboard Cite

In yeast, INO1 and CHO2 gene expression is subject to repression in response to inositol and choline supplementation. The response by both genes to inositol is controlled by a single set of regulatory factors and the highly conserved and repeated UASINO element (consensus: 5′ CATGTGAAAT 3′) that is found in multiple copies in both promoters. However, none of the native elements found in the INO1 and CHO2 promoters constitutes an exact match to the consensus element and the functionality of individual elements from these two promoters has not been tested. In this study, the function of individual putative UASINO elements from both promoters was tested by placing promoter fragments into a reporter construct which lacked a UAS element but contained the TATA element and start of transcription from the yeast CYC1 gene fused to the Escherichia coli lacZ gene. In addition, a set of oligonucleotides containing the consensus UASINO element with the first position systematically modified was also tested for UASINO function. These studies indicated that elements that contain a C or an A as the first base at the 5′ end are functional to varying degrees. The majority of potential UASINO elements from the INO1 promoter were found to be inactive, whereas all of the elements from the CHO2 promoter tested were active. These results are discussed in light of the differential regulation of the two promoters.

show abstract

Phospholipid Biosynthesis in Yeast

Cited by 321 publications

References 2 publications

Dimethyl Sulfoxide Exposure Facilitates Phospholipid Biosynthesis and Cellular Membrane Proliferation in Yeast Cells

Dimethyl Sulfoxide Exposure Facilitates Phospholipid Biosynthesis and Cellular Membrane Proliferation in Yeast Cells

Regulation of Phospholipid Synthesis in the Yeast cki1Δ eki1Δ Mutant Defective in the Kennedy Pathway

Functional characterization of the repeated UASINO element in the promoters of the INO1 and CHO2 genes of yeast

Contact Info

Product

Resources

About