MatA S. cerevisiae cells exposed to Iztli peptide 1 for 3.5, 7, 15 and 30 minutes
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ABSTRACT:
ORGANISM(S): Saccharomyces cerevisiae
PROVIDER: GSE83746 | GEO | 2016/06/28
SECONDARY ACCESSION(S): PRJNA326916
REPOSITORIES: GEO
Similar Datasets
Project description:Transcriptional profiling of MatA yeast cells exposed to a cationic antimicrobial peptide (Iztli peptide 1) for 3.5, 7, 15 and 30 min is compared with MatA yeast cells without the peptide Two-condition experiment, MatA cells with peptide (P) and without it (C). Biological samples: 4 control, 4 treatment, independently grown and harvested. Two replicates per array. Please note that [1] there is one raw data file per two replicates, as indicated in the sample description field [2] the Columns 10 and 11 (in the raw data file), labeled as Raw intensity (mean) T1C and Raw intensity (mean) T1P, correspond to the raw intensities for each spot. T1C correspond to control and T1P correspond to treatment with a peptide named Iztli Peptide 1 [3] The replicates can be located by sorting the column standard_name. Each row corresponds to a different gene, two rows for each gene, the first row corresponds to the replicate 1 and the second to the replicate 2.
2016-06-28 | E-GEOD-83746 | biostudies-arrayexpress
Project description:The mammalian gut secretes a family of multifunctional peptides that affect appetite, intestinal secretions, and motility, while some regulate the microbiota. We report peptide YY (PYY1-36), but not endocrine PYY3-36, is an antimicrobial peptide (AMP) expressed by gut epithelial Paneth Cells (PC). PC-PYY has limited antibacterial activity, but shows selective activity against virulent hyphal, but not yeast forms, of Candida albicans. 5 PC-PYY is a cationic molecule that interacts with the anionic surfaces of fungal hyphae to cause membrane disruption and transcriptional reprogramming to maintain the yeast phenotype of the fungus. PC-PYY is packaged into secretory granules and is secreted into and retained by surface mucus, which optimizes PC-PYY activity. Hence, PC-PYY acts as a selective antifungal AMP that contributes to the maintenance of gut fungal commensalism.
2024-02-28 | GSE229566 | GEO
Project description:Contains a collection of wildtype matA Saccharomyces cerevisiae strains for estimating the biological variation.
2012-11-14 | GSE42240 | GEO
Project description:Contains a collection of wildtype matA Saccharomyces cerevisiae strains for estimating the biological variation. Two channel microarrays were used. RNA isolated from a large amount of wt yeast from a single culture was used as a common reference. Two independent cultures were hybridized on two separate microarrays.
2012-11-14 | E-GEOD-42240 | biostudies-arrayexpress
Project description:Contains a collection of wildtype matA Saccharomyces cerevisiae strains grown using a Tecan platereader for estimating the biological variation.
2012-11-14 | GSE42241 | GEO
Project description:Contains a collection of wildtype matA Saccharomyces cerevisiae strains grown using a Tecan platereader for estimating the biological variation. Two channel microarrays were used. RNA isolated from a large amount of wt yeast from a single culture was used as a common reference. Two independent cultures were hybridized on two separate microarrays.
2012-11-14 | E-GEOD-42241 | biostudies-arrayexpress
Project description:Staphylococcus aureus is a leading cause of hospital-associated infections. In addition, highly virulent strains of methicillin-resistant S. aureus (MRSA) are currently spreading outside health care settings. Survival in the human host is largely defined by the ability of S. aureus to resist mechanisms of innate host defense, of which antimicrobial peptides form a key part especially on epithelia and in neutrophil phagosomes. Here we demonstrate that the antimicrobial-peptide sensing system aps of the standard community-associated MRSA strain MW2 controls resistance to cationic antimicrobial peptides. The core of aps-controlled resistance mechanisms comprised the D-alanylation of teichoic acids (dlt operon), the incorporation of cationic lysyl-phosphatidylglycerol (L-PG) in the bacterial membrane (mprF), and the vraF/vraG putative antimicrobial peptide transporter. Further, the observed increased production of L-PG under the influence of cationic antimicrobial peptides was accompanied by the up-regulation of lysine biosynthesis. In noticeable difference to the aps system of S. epidermidis, only selected antimicrobial peptides strongly induced the aps response. Heterologous complementation with the S. epidermidis apsS gene indicated that this is likely caused by differences in the short extracellular loop of ApsS that interacts with the inducing antimicrobial peptide. Our study shows that the antimicrobial peptide sensor system aps is functional in the important human pathogen S. aureus, significant interspecies differences exist in the induction of the aps gene regulatory response, and aps inducibility is clearly distinguishable from effectiveness towards a given antimicrobial peptide. Keywords: Wild type control vs treated vs mutant Wild type untreated in triplicate is compared to wild type treated in triplicate along with three mutants in triplicate with and without treatment of indolicidin, totalling 30 samples
2008-04-06 | E-GEOD-8400 | biostudies-arrayexpress
Project description:Staphylococcus aureus is a leading cause of hospital-associated infections. In addition, highly virulent strains of methicillin-resistant S. aureus (MRSA) are currently spreading outside health care settings. Survival in the human host is largely defined by the ability of S. aureus to resist mechanisms of innate host defense, of which antimicrobial peptides form a key part especially on epithelia and in neutrophil phagosomes. Here we demonstrate that the antimicrobial-peptide sensing system aps of the standard community-associated MRSA strain MW2 controls resistance to cationic antimicrobial peptides. The core of aps-controlled resistance mechanisms comprised the D-alanylation of teichoic acids (dlt operon), the incorporation of cationic lysyl-phosphatidylglycerol (L-PG) in the bacterial membrane (mprF), and the vraF/vraG putative antimicrobial peptide transporter. Further, the observed increased production of L-PG under the influence of cationic antimicrobial peptides was accompanied by the up-regulation of lysine biosynthesis. In noticeable difference to the aps system of S. epidermidis, only selected antimicrobial peptides strongly induced the aps response. Heterologous complementation with the S. epidermidis apsS gene indicated that this is likely caused by differences in the short extracellular loop of ApsS that interacts with the inducing antimicrobial peptide. Our study shows that the antimicrobial peptide sensor system aps is functional in the important human pathogen S. aureus, significant interspecies differences exist in the induction of the aps gene regulatory response, and aps inducibility is clearly distinguishable from effectiveness towards a given antimicrobial peptide. Keywords: Wild type control vs treated vs mutant
2008-04-07 | GSE8400 | GEO
Project description:Contains a collection of wildtype matA Saccharomyces cerevisiae strains for estimating the biological variation. Please refer to a related experiment where the yeast strains were grown in a platereader: E-MTAB-1351 (http://www.ebi.ac.uk/arrayexpress/experiments/E-MTAB-1351). Two other wildtype pool experiments have also been deposited in ArrayExpress previously. The experiments have similar setup as the current submission and E-MTAB-1351 (e.g. using matAlpha strains and also grown either using an erlenmeyer or using the Tecan platereader), but the pools are much larger and also used more frequently. The ArrayExpress accessions are: E-TABM-773 (matAlpha wildtype strains erlenmeyer growth, http://www.ebi.ac.uk/arrayexpress/experiments/E-TABM-773) and E-TABM-984 (matAlpha wildtype strains, tecan platereader growth, http://www.ebi.ac.uk/arrayexpress/experiments/E-TABM-984)
2012-11-13 | E-MTAB-1352 | biostudies-arrayexpress
Project description:Haploid budding yeast has two mating types, defined by the alleles of the MAT locus, MATa and MATα. Mating occurs when two haploid cells of opposite mating types signal to each other using reciprocal pheromones and receptors, polarize and grow towards each other, and eventually fuse to form a single diploid cell. The pheromones and receptors are necessary and sufficient to define a mating type, but other mating type-specific proteins make mating more efficient. We examined the role of these proteins by genetically engineering “transvestite” cells that swap the pheromone, pheromone receptor, and pheromone processing factors of one mating type for another. These cells can mate with each other, but their mating is inefficient. By characterizing their mating defects and examining their transcriptomes, we found Afb1 (a-factor barrier), a novel MATα-specific protein that interferes with a-factor, the pheromone secreted by MATa cells. We show that strong pheromone secretion is essential for efficient mating and that the weak mating of transvestites can be improved by boosting their pheromone production. Using synthetic biology, it is possible to characterize the factors that control efficiency in biological processes. In the case of budding yeast mating, selection for increased mating efficiency is likely to have continually boosted pheromone levels and the ability to discriminate between partners who make more (potentially fitter) and less (potentially less fit) pheromones. This sensitivity to which partner makes more pheromone comes at a cost: it means mating is not robust in situations where all potential partners make less pheromone.
2014-01-07 | GSE49372 | GEO