[URE3] Prion formation by the Candida albicans Ure2p (but not by C. glabrata Ure2p)-ScUre2
Ontology highlight
ABSTRACT:
ORGANISM(S): Saccharomyces cerevisiae
PROVIDER: GSE26611 | GEO | 2012/01/01
SECONDARY ACCESSION(S): PRJNA142195
REPOSITORIES: GEO
Similar Datasets
Project description:[URE3] is a prion (infectious protein) of the Saccharomyces cerevisiae Ure2p, a regulator of nitrogen catabolism. We find that the Ure2p of Candida albicans and C. glabrata also regulate nitrogen catabolism. Conservation of amino acid sequence within the prion domain of Ure2p has been proposed as evidence that the [URE3] prion helps its host. We show that the C. albicans Ure2p, which does not conserve this sequence, can nonetheless form a [URE3] prion, but the C. glabrata Ure2p, which does have the conserved sequence, cannot form [URE3]. These results suggest that the sequence is not conserved to preserve prion forming ability.
2012-01-01 | GSE26613 | GEO
Project description:[URE3] is a prion (infectious protein) of the Saccharomyces cerevisiae Ure2p, a regulator of nitrogen catabolism. We find that the Ure2p of Candida albicans and C. glabrata also regulate nitrogen catabolism. Conservation of amino acid sequence within the prion domain of Ure2p has been proposed as evidence that the [URE3] prion helps its host. We show that the C. albicans Ure2p, which does not conserve this sequence, can nonetheless form a [URE3] prion, but the C. glabrata Ure2p, which does have the conserved sequence, cannot form [URE3]. These results suggest that the sequence is not conserved to preserve prion forming ability.
2012-01-01 | GSE26612 | GEO
Project description:[URE3] is a prion (infectious protein) of the Saccharomyces cerevisiae Ure2p, a regulator of nitrogen catabolism. We find that the Ure2p of Candida albicans and C. glabrata also regulate nitrogen catabolism. Conservation of amino acid sequence within the prion domain of Ure2p has been proposed as evidence that the [URE3] prion helps its host. We show that the C. albicans Ure2p, which does not conserve this sequence, can nonetheless form a [URE3] prion, but the C. glabrata Ure2p, which does have the conserved sequence, cannot form [URE3]. These results suggest that the sequence is not conserved to preserve prion forming ability. Two groups (WT and ure2 mutant) consisted of 4 biological replicates in which a ure2 deleted strain sample was paired with the wild type strain sample. Each group included 1 reciprocally labeled sample.
2012-01-01 | E-GEOD-26611 | biostudies-arrayexpress
Project description:[URE3] is a prion (infectious protein) of the Saccharomyces cerevisiae Ure2p, a regulator of nitrogen catabolism. We find that the Ure2p of Candida albicans and C. glabrata also regulate nitrogen catabolism. Conservation of amino acid sequence within the prion domain of Ure2p has been proposed as evidence that the [URE3] prion helps its host. We show that the C. albicans Ure2p, which does not conserve this sequence, can nonetheless form a [URE3] prion, but the C. glabrata Ure2p, which does have the conserved sequence, cannot form [URE3]. These results suggest that the sequence is not conserved to preserve prion forming ability. Two groups (Wild type and ure2 mutants) consisted of 4 biological replicates in which a Ure2 mutant sample was paired with the wild type strain BG14 sample. Each group included 1 reciprocally labeled sample.
2012-01-01 | E-GEOD-26612 | biostudies-arrayexpress
Project description:[URE3] is a prion (infectious protein) of the Saccharomyces cerevisiae Ure2p, a regulator of nitrogen catabolism. We find that the Ure2p of Candida albicans and C. glabrata also regulate nitrogen catabolism. Conservation of amino acid sequence within the prion domain of Ure2p has been proposed as evidence that the [URE3] prion helps its host. We show that the C. albicans Ure2p, which does not conserve this sequence, can nonetheless form a [URE3] prion, but the C. glabrata Ure2p, which does have the conserved sequence, cannot form [URE3]. These results suggest that the sequence is not conserved to preserve prion forming ability. Two groups (WT and ure2 mutants) consisted of 4 biological replicates in which a ure2 deleted strain sample was paired with the wild type strain sample. Each group included 1 reciprocally labeled sample.
2012-01-01 | E-GEOD-26613 | biostudies-arrayexpress
Project description:This SuperSeries is composed of the following subset Series: GSE26611: [URE3] Prion formation by the Candida albicans Ure2p (but not by C. glabrata Ure2p)-ScUre2 GSE26612: [URE3] Prion formation by the Candida albicans Ure2p (but not by C. glabrata Ure2p)-CgUre2 GSE26613: [URE3] Prion formation by the Candida albicans Ure2p (but not by C. glabrata Ure2p)-CaUre2 Refer to individual Series
2012-01-01 | E-GEOD-26620 | biostudies-arrayexpress
Project description:Metabolic adaption to different host niches is one of the most important virulence traits of human fungal pathogens. The metabolic versatility of fungi and other cellular processes such as proliferation, morphogenesis and stress responses are tightly regulated by complex networks in which protein kinases play a crucial role. Serine-arginine (SR) protein kinases are highly conserved in all eukaryotes, but their function in pathogenic Candida spp. has not yet been investigated. C. albicans genome encodes two (Sky1, Sky2) and Candida glabrata one (Sky1) homolog of the human SR protein kinase 1 (SRPK1). We utilized deletion strains of the respective genes in both fungi in order to examine their cellular functions. C. glabrata and C. albicans strains lacking SKY1 exhibited higher resistance to osmotic stress and toxic polyamine concentrations to their ortholog in the model yeast Saccharomyces cerevisiae Sky1. Deletion of SKY2 in C. albicans resulted in impaired utilization of dipeptides as the sole nitrogen source. Subsequent phosphoproteomic analysis identified Ptr22, a transporter of di- and tri-peptides in C. albicans, as a potential Sky2 substrate. Overexpression of PTR22 in the sky2∆ restored the ability to grow on dipeptides as the sole nitrogen source and rendered the cells more susceptible to the dipeptide antibiotics Polyoxin D and Nikkomycin Z. Altogether, our results demonstrate that the two SR-like protein kinases in C. albicans have divergent functions: C. albicans and C. glabrata Sky1 is functionally similar to Sky1 in S. cerevisiae, whereas Sky2 regulates uptake of dipeptides.
2022-05-09 | PXD027612 | Pride
Project description:Metabolic pathways are largely conserved in eukaryotes, but the transcriptional regulation of these pathways can sometimes vary between species; this has been termed rewiring. Recently it has been established that in the Saccharomyces lineage starting from Saccharomyces castelli, genes involved in allantoin breakdown have been genomically relocated to form the DAL cluster. The formation of the DAL cluster occurred along with the loss of urate permease (UAP) and urate oxidase (UOX), reducing the requirement for oxygen and bypassing the candidate Ppr1 inducer, uric acid. In Saccharomyces cerevisiae this allantoin catabolism cluster is regulated by the transcription factor Dal82, which is not present in many of the pre-rearrangement fungal species. We have used ChIP-Chip analysis, transcriptional profiling of an activated Ppr1 protein, bioinformatics, and nitrogen utilization studies, to establish that in Candida albicans the zinc cluster transcription factor Ppr1 controls this allantoin catabolism regulon. Intriguingly, in S. cerevisiae the Ppr1 ortholog binds the same DNA motif (CGG(N6)CCG) as in C. albicans, but serves as a regulator of pyrimidine biosynthesis. This transcription factor rewiring appears to have taken place at the same phylogenetic step as the formation of the rearranged DAL cluster. This transfer of the control of allantoin degradation from Ppr1 to Dal82, together with the repositioning of Ppr1 to the regulation of pyrimidine biosynthesis, may have resulted from a switch to a metabolism that could exploit hypoxic conditions in the lineage leading to S. castellii and S. cerevisiae. Metabolic pathways are largely conserved in eukaryotes, but the transcriptional regulation of these pathways can sometimes vary between species; this has been termed rewiring. Recently it has been established that in the Saccharomyces lineage starting from Saccharomyces castelli, genes involved in allantoin breakdown have been genomically relocated to form the DAL cluster. The formation of the DAL cluster occurred along with the loss of urate permease (UAP) and urate oxidase (UOX), reducing the requirement for oxygen and bypassing the candidate Ppr1 inducer, uric acid. In Saccharomyces cerevisiae this allantoin catabolism cluster is regulated by the transcription factor Dal82, which is not present in many of the pre-rearrangement fungal species. We have used ChIP-Chip analysis, transcriptional profiling of an activated Ppr1 protein, bioinformatics, and nitrogen utilization studies, to establish that in Candida albicans the zinc cluster transcription factor Ppr1 controls this allantoin catabolism regulon. Intriguingly, in S. cerevisiae the Ppr1 ortholog binds the same DNA motif (CGG(N6)CCG) as in C. albicans, but serves as a regulator of pyrimidine biosynthesis. This transcription factor rewiring appears to have taken place at the same phylogenetic step as the formation of the rearranged DAL cluster. This transfer of the control of allantoin degradation from Ppr1 to Dal82, together with the repositioning of Ppr1 to the regulation of pyrimidine biosynthesis, may have resulted from a switch to a metabolism that could exploit hypoxic conditions in the lineage leading to S. castellii and S. cerevisiae.
2016-04-15 | GSE80341 | GEO
Project description:Metabolic pathways are largely conserved in eukaryotes, but the transcriptional regulation of these pathways can sometimes vary between species; this has been termed rewiring. Recently it has been established that in the Saccharomyces lineage starting from Saccharomyces castelli, genes involved in allantoin breakdown have been genomically relocated to form the DAL cluster. The formation of the DAL cluster occurred along with the loss of urate permease (UAP) and urate oxidase (UOX), reducing the requirement for oxygen and bypassing the candidate Ppr1 inducer, uric acid. In Saccharomyces cerevisiae this allantoin catabolism cluster is regulated by the transcription factor Dal82, which is not present in many of the pre-rearrangement fungal species. We have used ChIP-Chip analysis, transcriptional profiling of an activated Ppr1 protein, bioinformatics, and nitrogen utilization studies, to establish that in Candida albicans the zinc cluster transcription factor Ppr1 controls this allantoin catabolism regulon. Intriguingly, in S. cerevisiae the Ppr1 ortholog binds the same DNA motif (CGG(N6)CCG) as in C. albicans, but serves as a regulator of pyrimidine biosynthesis. This transcription factor rewiring appears to have taken place at the same phylogenetic step as the formation of the rearranged DAL cluster. This transfer of the control of allantoin degradation from Ppr1 to Dal82, together with the repositioning of Ppr1 to the regulation of pyrimidine biosynthesis, may have resulted from a switch to a metabolism that could exploit hypoxic conditions in the lineage leading to S. castellii and S. cerevisiae.
2016-04-06 | GSE79931 | GEO
Project description:We investigated different escape and defense strategies of Candida glabrata and Candida albicans against the natural fungivorous predator Protostelium aurantium using dual RNA-Seq. While C. albicans was found to be very succesfull in preventing from amoeba recognition, C. glabrata in turn, was rapidly taken up but remained undigested with a comparably low transcriptional activity. Trophozoites of the amoeba Protostelium aurantium were fed seperately with the two fungal species and samples for RNA isolation were taken at time points 0 min (control), 30 min and 60 min. At indicated time points samples were shock frozen and used for RNA isolation. Samples for RNAseq were taken at time points 0 min (control), 30 min and 60 min. RNA samples from identical timepoints for C. albicans and C. glabrata were pooled for RNA sequencing. We investigated different escape and defense strategies of Candida spp. against natural fungivorous predator. While C. parapsilosis underwent rapid predation and intracellular killing of the yeast, C. albicans was found to be very succesfull in preventing from amoeba recognition. C. glabrata in turn, was rapidly taken up but remained undigested with a comparably low transcriptional activity.
2018-09-01 | GSE116533 | GEO