Relative roles of Stp1 and Stp2 in amino acid and peptide utilization in Candida albicans
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA607573 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR11116124.fastq.gz | Fastqsanger.gz | |||
| SRR11116125.fastq.gz | Fastqsanger.gz | |||
| SRR11116126.fastq.gz | Fastqsanger.gz | |||
| SRR11116127.fastq.gz | Fastqsanger.gz | |||
| SRR11116128.fastq.gz | Fastqsanger.gz |
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Project description:Candida albicans is a member of the normal commensal flora with the ability to cause disease in susceptible individuals. Nutrient acquisition is of central importance for C. albicans to colonize and thrive in the host. We have previously assessed the role of amino acid utilization for growth and manipulation of pH, triggering the filamentation program and promoting immune evasion. While the role of amino acids has been largely studied, protein utilization has remained less well understood. We investigated the utilization of peptides as a source of carbon and to support the neutralization phenomena. We found that both transcription factors Stp1 and Stp2 are required for proper peptide utilization in a manner dependent of amino acid sensing signaling involving the SPS system. However, we found that Stp2 is the major contributor for this process. Epistasis experiments shown that Stp1 partially restores the ability to utilize peptides in the absence of amino acid signaling, whilst Stp2 is sufficient to fully restore this phenotype. Transcriptomic analysis revealed that the response to amino acids and peptides is very similar, but peptides represent a more difficult carbon source to utilize. It is known that the Stp1/Stp2 duet has divergent roles in C. albicans, however the specific set of genes controlled by each TF remained unclear. We showed that the Stp1 regulon is limited to two oligopeptide transporters (OPT1, OPT9), and iron-acquisition oxidoreductase (CFL2), a nucleoside transporter (NUP) and a leucine aminopeptidase (APE2), whereas Stp2 is responsible for the regulation of amino acid uptake and catabolic genes, in a manner dependent of amino acid sensing. Surprisingly, Stp2 affects expression of genes involved in the filamentation response (e.g. UME6, SFL2) that have been associated with host colonization. In a GI tract competition experiment, mutants lacking the amino acid sensor Ssy1 or the TF Stp2 exhibited decreased colonization, while an stp1Δ/Δ mutant showed increase colonization. Taken together, these results highlight the importance of peptide and amino acid utilization for colonization of the host, a prerequisite for disseminated disease.
2020-02-20 | GSE145576 | GEO
Project description:Purpose of this study was to define the transcriptional response of Candida albicans to the utilization of amino acids as the sole carbon source (C-source) in order to study regulation of metabolic adaptation of the fungus to amino acid-rich media. Furthermore, potential regulatory activities of the transcription factor Stp2 exceeding the described role in amino acid-uptake have been investigated. Therefore, the SC5314 wild type and a deletion strain of Stp2 (stp2Δ) were incubated in medium containing either glucose (SD) or a mixture of proteinogenioc amino acids (SC) as the sole C-source and the cellular transcriptome defined using RNA-sequencing.
2025-10-07 | GSE277530 | GEO
Project description:Transcriptional response of Candida albicans to the utilization of amino acids as the sole carbon source
| PRJNA1162727 | ENA
Project description:Lantibiotics are highly modified peptides that are part of the bacteriocin family of antimicrobial peptides. We have identified a Phr peptide quorum sensing system (TprA/PhrA) that controls the expression of a lantibiotic gene cluster in the Gram-positive human pathogen, Streptococcus pneumoniae. We have characterized the basic mechanism for a Phr peptide signaling system in S. pneumoniae D39 and found that it induces expression of the lantibiotic genes when pneumococcal cells are at high density in the presence of galactose, a main sugar of the human nasopharynx, a highly competitive microbial environment. In this study we used RNA-seq analysis to examine the changes in relative transcript amounts caused by ∆tprA and ∆phrA mutations or the addition of the 10-residue synthetic PhrA peptide. These analyses reveal that PhrA peptide addition induces the transcription of a cluster of lantibiotic gene that appear to process and provide immunity to a lantibiotic peptide. In addition, TprA, a transcriptional factor regulated by a Phr peptide, autoregulates its own transcription.
2015-10-20 | GSE68598 | GEO
Project description:Control of citrate utilization by Candida albicans Adr1
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Project description:We investigated the transcriptome profile of HEK293T cells transfected with a plasmid encoding 9J10, a peptide isolated in a phenotypic screen from a library of peptides derived from bacterial and archaeal genomes. The peptide was identified in a screen for FOXO3a reactivation and has been shown to interact with 14-3-3 proteins and induce relocalisation of FOXO3a from the cytoplasm to the nucleus. A peptide with a single amino acid mutation does not interact with 14-3-3 and was included as a control. A constitutively active FOXO3a mutant was also included as a control.
2021-05-28 | E-MTAB-10161 | biostudies-arrayexpress
Project description:phytoplankton exudate utilization by bacteria
| PRJEB44710 | ENA
Project description:D-Glutamate (D-Glu), an essential component of peptidoglycans, can be utilized as carbon and nitrogen source by Pseudomonas aeruginosa. DNA microarrays were employed to identify genes involved in D-Glu catabolism. Through gene knockout and growth phenotype analysis, the divergent dguR-dguABC (D-glutamate utilization) gene cluster was shown to participate in D-Glu catabolism and regulation. The dguA gene encodes a FAD-dependent D-amino acid dehydrogenase with D-Glu as its preferred substrate, and its promoter was specifically induced by exogenous D-Glu and D-Gln. The function of DguR as transcriptional activator of the dguABC operon was demonstrated by promoter activity measurements in vivo and by mobility shift assays with purified His-tagged DguR in vitro. Although the DNA-binding activity of DguR did not require D-Glu, the presence of D-Glu in the binding reaction was found to stabilize a preferred nucleoprotein complex. The dguB gene encodes a putative enamine/imine deaminase of the RidA family, but its role in D-Glu catabolism remained to be determined. While a lesion in dguC encoding a periplasmic solute binding protein did not affect growth on D-Glu, the AatJMQP transporter for acidic amino acid uptake was found essential for D-Glu and L-Glu utilization. Expression of this uptake system was subjected to induction by exogenous DL-Glu, most likely via the AauSR two-component system. In summary, DguA was identified in this study as a new member of the FAD-dependent amino acid dehydrogenase family for D-amino acid catabolism. DguR serves as a D-Glu sensor and transcriptional activator of the dguA promoter. Pseudomonas aeruginosa PAO1 was chosen as model to study gene response with different D-amino acids.
2013-05-03 | E-GEOD-46603 | biostudies-arrayexpress
Project description:Opportunistic fungal pathogen Candida albicans often encounters host niches where it must survive on alternative carbon sources alone. In Saccharomyces cerevisiae, transcription factor Adr1 activates genes required for acetate and glycerol utilization. However, previous researchers found that CaADR1 deletion mutants have robust growth on acetate and glycerol. We have found that Adr1 is required for growth on citrate. This phenotype is manifested among multiple strains isolated from all known host niches. RNA sequencing analyses of adr1Δ/Δ and wild-type strains show that Adr1 is required for expression of genes within the TCA cycle and gluconeogenesis. Major targets include enzymes Mdh1 and Pck1. Unexpectedly, one of the most downregulated genes is not within the central metabolic pathway. HGT17 is a putative glucose transporter. Phenotypic analyses support the hypothesis that Hgt17 is able to transport citrate.
2025-05-05 | GSE287330 | GEO
Project description:D-Glutamate (D-Glu), an essential component of peptidoglycans, can be utilized as carbon and nitrogen source by Pseudomonas aeruginosa. DNA microarrays were employed to identify genes involved in D-Glu catabolism. Through gene knockout and growth phenotype analysis, the divergent dguR-dguABC (D-glutamate utilization) gene cluster was shown to participate in D-Glu catabolism and regulation. The dguA gene encodes a FAD-dependent D-amino acid dehydrogenase with D-Glu as its preferred substrate, and its promoter was specifically induced by exogenous D-Glu and D-Gln. The function of DguR as transcriptional activator of the dguABC operon was demonstrated by promoter activity measurements in vivo and by mobility shift assays with purified His-tagged DguR in vitro. Although the DNA-binding activity of DguR did not require D-Glu, the presence of D-Glu in the binding reaction was found to stabilize a preferred nucleoprotein complex. The dguB gene encodes a putative enamine/imine deaminase of the RidA family, but its role in D-Glu catabolism remained to be determined. While a lesion in dguC encoding a periplasmic solute binding protein did not affect growth on D-Glu, the AatJMQP transporter for acidic amino acid uptake was found essential for D-Glu and L-Glu utilization. Expression of this uptake system was subjected to induction by exogenous DL-Glu, most likely via the AauSR two-component system. In summary, DguA was identified in this study as a new member of the FAD-dependent amino acid dehydrogenase family for D-amino acid catabolism. DguR serves as a D-Glu sensor and transcriptional activator of the dguA promoter.
2013-05-03 | GSE46603 | GEO