Effect of the culture medium on the degradation of nucleotide triphosphates
Ontology highlight
ABSTRACT: The effect of the Verduyn culture medium on the degradation profiles of nucleotide triphosphates extracted under typical boiling ethanol conditions was evaluated.
Project description:The influence of particular groups of compounds/metabolites, mainly comprising major central carbon metabolites including amino acids, organic acids, sugar phosphates, coenzymes, etc, on the degradation profiles of nucleotide triphosphates extracted under typical boiling ethanol conditions was evaluated.
Project description:The effect of a complex cellular matrix extracted from yeast (S. cerevisiae, strain YSBN6 (MATa; genotype: FY3 ho::HphMX4 derived from the S288C parental strain)) on the degradation profiles of nucleotide triphosphates extracted under typical boiling ethanol conditions was evaluated.
Project description:The degradation kinetics of nucleotide triphosphates (ATP, GTP, UTP and CTP) were evaluated under boiling ethanol extraction conditions (95°C) during 0 to 300 minutes.
Project description:Cells maintain proteostasis by selectively recognizing and targeting misfolded proteins for degradation. In Saccharomyces cerevisiae, the Hsp70 nucleotide exchange factor Fes1 is essential for the degradation of chaperone-associated misfolded proteins by the ubiquitin-proteasome system. Here we show that the FES1 transcript undergoes unique 3' alternative splicing that results in two equally active isoforms with alternative C-termini, Fes1L and Fes1S. Fes1L is actively targeted to the nucleus and represents the first identified nuclear Hsp70 nucleotide exchange factor. In contrast, Fes1S localizes to the cytosol and is essential to maintain proteostasis. In the absence of Fes1S, the heat-shock response is constitutively induced at normally non-stressful conditions. Moreover, cells display severe growth defects when elevated temperatures, amino acid analogues or the ectopic expression of misfolded proteins, induce protein misfolding. Importantly, misfolded proteins are not targeted for degradation by the ubiquitin-proteasome system. These observations support the notion that cytosolic Fes1S maintains proteostasis by supporting the removal of toxic misfolded proteins by proteasomal degradation. This study provides key findings for the understanding of the organization of protein quality control mechanisms in the cytosol and nucleus. 4 strains (WT, fes1Î, fes1ÎS, fes1ÎL) were sequenced in triplicates from independent RNA isolations.
Project description:To identify ethanol-induced genes, gene expression profile between arabidopis seedlings grown on MS medium with and without ethanol using the custom microarray (GPL22706) were analyzed.
Project description:The role of transcription factor Mxr1p has so far been studied in methanol, amino acid and acetate metabolism. We have demonstrated a key role of Mxr1p in regulation of ethanol metabolism when cells are cultured in medium containing ethanol as sole carbon source. We employed RNA Seq to identify new targets of Mxr1p in medium containing ethanol.
Project description:Cells maintain proteostasis by selectively recognizing and targeting misfolded proteins for degradation. In Saccharomyces cerevisiae, the Hsp70 nucleotide exchange factor Fes1 is essential for the degradation of chaperone-associated misfolded proteins by the ubiquitin-proteasome system. Here we show that the FES1 transcript undergoes unique 3' alternative splicing that results in two equally active isoforms with alternative C-termini, Fes1L and Fes1S. Fes1L is actively targeted to the nucleus and represents the first identified nuclear Hsp70 nucleotide exchange factor. In contrast, Fes1S localizes to the cytosol and is essential to maintain proteostasis. In the absence of Fes1S, the heat-shock response is constitutively induced at normally non-stressful conditions. Moreover, cells display severe growth defects when elevated temperatures, amino acid analogues or the ectopic expression of misfolded proteins, induce protein misfolding. Importantly, misfolded proteins are not targeted for degradation by the ubiquitin-proteasome system. These observations support the notion that cytosolic Fes1S maintains proteostasis by supporting the removal of toxic misfolded proteins by proteasomal degradation. This study provides key findings for the understanding of the organization of protein quality control mechanisms in the cytosol and nucleus.
Project description:We have previously shown that fed-batch processes with the longest uncoupling phase (ethanol adapted) were characterized by induction of storage carbohydrates, a metabolic event typical of yeast cells experiencing nutrient limitation, at the onset of this phase, whereas this metabolic event was not seen in processes with a short uncoupling phase (ethanol non adapted culture). Taken together, our results suggested that reproducible high bioethanol performance in aerated fed-batch process may be linked to the ability of yeast cells to impede ethanol toxicity by triggering a metabolic remodelling reminiscent to that of cells entering a quiescent G0/G1 state. The aim of this study was to search for genes implicated in the induction an ethanol adapted culture vs ethanol non-adapted culture.
Project description:Human umbilical vein endothelial cells (HUVEC) were cultured in serum-free medium with 50 μmol/L ADMA (ADMA group) or without ADMA (NA group ). Asymmetric dimethylarginine is a typical uremic toxin which used to induce HUVEC injury.
Project description:The mice stool samples were collected for culturing with different medium for understanding the role of different medium component on the microbiome.