Dataset Information

Transcript profiling of Candida albicasn gtr1/gtr1 mutant

ABSTRACT: The Target of Rapamycin complex (TORC1) is an essential regulator of metabolism in eukaryotic cells and in the fungal pathogen C. albicans regulates morphogenesis and nitrogen acquisition. Gtr1 encodes a highly conserved GTPase which in S. cerevisiae regulates nitrogen sensing and TORC1 activation. Here, were characterize the role of C. albicans GTR1 in TORC1 activation and compare with the previously characterized GTPase Rhb1. A homozygous gtr1/gtr1 mutant exhibited impaired TORC1-mediated phosphorylation of Ribosomal Protein S6 and increased susceptibility to rapamycin. Overexpression of GTR1 impaired nitrogen starvation induced filamentous growth, MEP expression and growth in BSA as the sole nitrogen source. Both GTR1 and RHB1 were shown to regulate genes involved in ribosome biogenesis, amino acid biosynthesis and expression of biofilm-growth induced genes. The rhb1/rhb1 mutant exhibited a different pattern of expression of Sko1 regulated genes and increased susceptibility to Congo Red and Calcofluor white. The homozygous gtr1/gtr1 mutant exhibited enhanced flocculation phenotypes and similar to the rhb1/rhb1 mutant exhibited enhanced biofilm formation on plastic surfaces. In summary, Gtr1 and Rhb1 link nutrient sensing and biofilm formation and this connectivity may have evolved to enhance competitiveness of C. albicans in niches where there is intense competition with other microbes for space and nutrients.

ORGANISM(S): Candida albicans

PROVIDER: GSE104160 | GEO | 2017/09/23

SECONDARY ACCESSION(S): PRJNA411838

REPOSITORIES: GEO

ACCESS DATA

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Project description:We show that the sensitivity of tsc mutant cells to rapamycin is mediated by TORC1 and can be suppressed by overexpression of the 2-oxoglutarate-Fe(II) dependent oxygenase, Isp7. We show that Isp7 is a novel regulator of amino acids uptake that acts via regulation of gene expression, both upstream and downstream of TOR signaling. suppressed by overexpression of the putative 2-oxoglutarate-Fe(II) dependent oxygenase, Isp7. We show that Isp7 is a novel master regulator of amino acids uptake that acts via regulation of gene expression, both upstream and downstream of TOR signaling. TOR proteins reside in two distinct complexes, TOR complex 1 and 2 (TORC1 and TORC2) that are central for the regulation of cellular growth, proliferation and survival. TOR is also the target for the immunosuppressive and anti-cancer drug rapamycin. In Schizosaccharaomyces pombe, disruption of the TSC complex, mutations in which can lead to the Tuberous Sclerosis syndrome in humans, results in a rapamycin sensitive phenotype under poor nitrogen conditions. We show here that the sensitivity to rapamycin is mediated via inhibition of TORC1 and suppressed by overexpression of isp7+, a member of the family of 2-oxoglutarate-Fe(II) dependent oxygenases. The transcript level of isp7+ is negatively regulated by TORC1 but positively regulated by TORC2. Yet, we find extensive similarity between the transcriptome of cells disrupted for isp7+ and cells mutated in the catalytic subunit of TORC1. Moreover, Isp7 regulates amino acid permease expression similarly to TORC1 and in contrast to TORC2. Overexpression of isp7+ induces TORC1-dependent phosphorylation of ribosomal protein Rps6, while inhibiting TORC2-dependent phosphorylation and activation of the AGC-like kinase Gad8. Taken together, our findings suggest a central role for Isp7 in amino acid homeostasis and the presence of isp7+-dependent regulatory loops that affect both TORC1 and TORC2. 6 Samples (arrays) were performed. We generated pairwise comparison between DISP7 and WT, using Partek Genomics Suite. Genes with pâ¤5%[FDR] and a fold-change difference of â¥2\1.5 or <-2\-1.5 were selected.

Dataset Information

Transcript profiling of Candida albicasn gtr1/gtr1 mutant

Dataset's files

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets