The accumulation and intracellular distribution of biological sulfoninum compounds in yeast

Schlenk, F.; Dainko, J. L.; Svihla, G.

doi:10.1016/0003-9861(70)90027-5

Cited by 26 publications

(16 citation statements)

References 21 publications

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“…Because SAM can be stored in vacuoles (Chan and Appling, 2003; Schlenk et al, 1970), we examined how disruption of two vacuolar proteins (Vtc1 and Vps33) that reportedly affect SAM homeostasis would affect SAM levels in cho2Δ cells. While deletion of VTC1 had little effect, deletion of VPS33 led to further accumulation of SAM in cho2Δ (Figures S7E).…”

Section: Resultsmentioning

confidence: 99%

A Metabolic Function for Phospholipid and Histone Methylation

et al. 2017

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SUMMARY S-adenosylmethionine (SAM) is the methyl donor for biological methylation modifications that regulate protein and nucleic acid functions. Here we show that methylation of a phospholipid, phosphatidylethanolamine (PE), is a major consumer of SAM. The induction of phospholipid biosynthetic genes is accompanied by induction of the enzyme that hydrolyzes S-adenosylhomocysteine (SAH), a product and inhibitor of methyltransferases. Beyond its function for the synthesis of phosphatidylcholine (PC), the methylation of PE facilitates the turnover of SAM for the synthesis of cysteine and glutathione through transsulfuration. Strikingly, cells that lack PE methylation accumulate SAM, which leads to hypermethylation of histones and the major phosphatase PP2A, dependency on cysteine, and sensitivity to oxidative stress. Without PE methylation, particular sites on histones then become methyl sinks to enable the conversion of SAM to SAH. These findings reveal an unforeseen metabolic function for phospholipid and histone methylation intrinsic to the life of a cell.

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Section: Resultsmentioning

confidence: 99%

A Metabolic Function for Phospholipid and Histone Methylation

et al. 2017

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“…The data on the size of the vacuolar pools of nucleosides are very scarce. It is known only that 60-90% of intracellular S-adenosyl-L-methionine is localized in the vacuolar compartment of the C. utilis cell (Schlenk et al, 1970).…”

Section: Discussionmentioning

confidence: 99%

Transport of organic acid anions and guanosine into vacuoles of Saccharomyces pastorianus

Kulakovskaya

Matys

Okorokov

1991

Yeast

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Isolated vacuoles of the yeast Saccharomyces pastorianus accumulate citrate, α‐ketoglutarate, malate and guanosine. This accumulation is Mg ATP‐dependent and inhibited by protonophores. The ionophores monensin and A23187 (electroneutral Men+/nH+‐exchange) inhibit guanosine accumulation but fail to block citrate uptake. Mg2+ ions (2 mM) increase the values of both Δ\documentclass{article}\pagestyle{empty}\begin{document}$ \tilde \mu $\end{document}H+ components and stimulate the uptake of all the above compounds. Ca2+ ions (1 mM), hyperpolarizing the yeast vacuolar membrane and dissipating the pH gradient, inhibit guanosine uptake and stimulate that of citrate. It is concluded that guanosine is transported into yeast vacuoles by an H+/guanosine antiporter while citrate, malate and α‐ketoglutarate are translocated by a uniporter(s) at the expense of the membrane potential (positive inside).

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“…The resulting plasmid was named p⌬CHS1. p⌬CHS1 DNA was used as a template in a PCR 3 with oligonucleotides 5Ј-GGC-CTACCGGACCTTGCAGTA-3Ј and 5Ј-TGAGGCCT-TACTGGTCATTAAGG-3Ј that amplify the whole disruption cassette. The amplicon had 700 bp of 5Ј end and 500 bp of 3Ј end of CHS1 gene and flanking regions available for homologous recombination with the genomic CHS1 copy.…”

Section: Construction Of Chitin Synthase Deletionsmentioning

confidence: 99%

“…Because of the popularity of the yeast Saccharomyces cerevisiae as a model for eukaryotic cell biology, several of the techniques developed for cell permeabilization have used this organism. Thus, permeabilized yeast cells have been obtained by treatment with small basic proteins (3,4) or chitosan (5) or with detergents (6).…”

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confidence: 99%