Dataset Information

Identification of distinct active pools of yeast serine palmitoyltransferase in sub-compartments of the ER.

ABSTRACT: Whole cell lysate proteome of ypk2D cells to WT cells and ypk2D YPK1-linker-CAAX cells to ypk2D cells

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Florian Fröhlich

LAB HEAD: Florian Fröhlich

PROVIDER: PXD047435 | Pride | 2023-12-01

REPOSITORIES: pride

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Identification of distinct active pools of yeast serine palmitoyltransferase in sub-compartments of the ER.

Esch Bianca M BM Walter Stefan S Schmidt Oliver O Fröhlich Florian F

Journal of cell science 20231219 23

Sphingolipids (SPs) are one of the three major lipid classes in eukaryotic cells and serve as structural components of the plasma membrane. The rate-limiting step in SP biosynthesis is catalyzed by the serine palmitoyltransferase (SPT). In budding yeast (Saccharomyces cerevisiae), SPT is negatively regulated by the two proteins, Orm1 and Orm2. Regulating SPT activity enables cells to adapt SP metabolism to changing environmental conditions. Therefore, the Orm proteins are phosphorylated by two s ...[more]

PMID: 37982431

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Project description:Treatment failures of antibiotic therapy are of major concern and can be caused by a misalignment of the antibiotic susceptibility determined in vitro with the behaviour of the pathogen in the patient. The aim of this study was to investigate the transcriptomic response of the uropathogenic strain E. coli CFT073 to antibiotic treatment in blood stream infection (BSI) models in order to understand and avoid antibiotic therapy failures in urosepsis treatments. Blood stream infection models were established by growing E. coli CFT073 in pooled human serum with and without ciprofloxacin and compared to Iso-sensitest medium. The antibiotic challenge was introduced at mid-logarithmic phase of growth of the organism to depict a clinical scenario . Global gene expression profiling of these conditions was examined using commercial DNA microarrays. The organismâs metabolic genes appeared to be regulated differently in each medium, this indicated that the bacterial growth regulation were different between the models. Bacterial growth in human serum mainly involved regulations of amino acid synthesis/utilisation such as glycine, arginine, thiamine, regulations of fimbrial proteins and bacteriophage genes. When comparing the responses to antibiotic challenge, bacteria grown in the respective medium displayed specific responses to the antibiotic challenge which were not seen in the other media. The common functions of genes that responded to the ciprofloxacin challenge were SOS response, DNA repair, DNA replication, fimbrial genes and bacteriophage initiation. A subset of the bacteriophage genes showed similar responses between the three models. From genes that were differentially regulated, responses observed in the serum model appeared to have the highest fold changes. In this study we established new models to investigate blood stream infections. They have been used to identify previously unknown differences in the molecular response to antibiotic treatment by the uropathogenic E. coli CFT073 depending on the media. These unique responses will help to unravel the complexity of bloodstream infection and can help to improve the antibiotic therapy that is used. A 20 array study using total RNA recovered from bacteria from bacteria that were either grown in human serum or Iso-Sensitest (IST) broth, with and without ciprofloxacin challenge. Arrays were performed in 5 biological replicates from each condition.Upon QC checks, certain biological repeats were excluded due to poor hybridisation results.

			Action	DRS
	1_1_WT_20221219161831.raw	Raw
	1_2_WT_20221219192043.raw	Raw
	1_3_WT_20221219222251.raw	Raw
	2_1_ypk2D.raw	Raw
	2_2_ypk2D.raw	Raw

Dataset Information

Identification of distinct active pools of yeast serine palmitoyltransferase in sub-compartments of the ER.

Dataset's files

Publications

Identification of distinct active pools of yeast serine palmitoyltransferase in sub-compartments of the ER.

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