ABSTRACT: Expression analysis of Candida glabrata CBS138 delta-cnb1, delta-crz1, delta-slt2, and delta-ire1 mutants in response to tunicamycin exposure (Transcriptional response of Candida glabrata to tunicamycin exposure)
Project description:Investigation of whole genome gene expression level changes in response to tunicamycin, an inhibitor of protein N-glycosylation, in Candida glabrata CBS138 delta-cnb1, delta-crz1, delta-slt2, and delta-ire1 mutants, compared to the wild-type strain. The mutations engineered into these strains render them hypersusceptible to tunicamycin. The mutants analyzed in this study are further described in Miyazaki, T. et al. (2010) Antimicrob Agents Chemother. 54(4):1639-1643 (PMID: 20100876) and Miyazaki, T. et al. (2010) FEMS Yeast Res 10(3):343-352, 2010 (PMID: 20214686). A fifteen chip study using total RNA isolated from Candida glabrata wild-type control and four mutant strains, in which the entire ORFs of CNB1 (XP_448800), CRZ1 (XP_449644), SLT2 (XP_447735), or IRE1 (XP_446111) are deleted. Each chip measures the expression level of 5,217 genes from Candida glabrata CBS138 with six 60-mer-probe pairs per gene, with two-fold technical redundancy.
Project description:Investigation of whole genome gene expression level changes in response to tunicamycin, an inhibitor of protein N-glycosylation, in Candida glabrata CBS138 delta-cnb1, delta-crz1, delta-slt2, and delta-ire1 mutants, compared to the wild-type strain. The mutations engineered into these strains render them hypersusceptible to tunicamycin. The mutants analyzed in this study are further described in Miyazaki, T. et al. (2010) Antimicrob Agents Chemother. 54(4):1639-1643 (PMID: 20100876) and Miyazaki, T. et al. (2010) FEMS Yeast Res 10(3):343-352, 2010 (PMID: 20214686).
Project description:Investigation of whole genome gene expression level changes in Candida glabrata CBS138 delta-vph2 mutant, compared to the wild-type strain in SC broth (pH5.0 and pH7.4). VPH2 gene encodes a protein that is the assembly factor of a functional V-ATPase. Loss of Vph2p leads to loss of a functional V-ATPase enzyme complex.
Project description:Candida glabrata lab strain BG2 was used as parent to obtain some aneuploids by exposure to tunicamycin. Transcriptomes of 9 aneuploids bearing different chromosome change were compared to parent BG2
Project description:Candida glabrata strain BG2 was exposed to ER stress inducer tunicamycin (8μg/ml). One adaptor (TJ255) was petite. Transcriptomes of TJ255 and BG2 were compared.
Project description:Approximately 1 million cells of Candida glabrata lab strian BG2 were spread on YPD plate supplemented with 8 ug/ml tunicamycin. Randomly 30 adaptors were chosen. 28 adpators were more tolerant than parent to tunicamycin. These 28 tolerant adaptors, as well as the parent BG2 were sequenced.
Project description:To examine the role of a glycosylphosphatidylinositol-linked aspartyl protease, CgYps1, in the regulation of pH homeostasis in Candida glabrata, transcriptional profiling analysis was carried out on wild-type and Cgyps1∆ cells grown in YNB medium (pH 5.5) and in YNB medium adjusted to pH 2.0. Genes involved in carbohydrate and amino acid metabolism, protein folding and stress response pathways were found to be differentially regulated in response to acidic environment in both the strains. To examine the role of a glycosylphosphatidylinositol-linked aspartyl protease, CgYps1, in the regulation of pH homeostasis in Candida glabrata, transcriptional profiling analysis was carried out on wild-type and Cgyps1∆ delta cells grown in YNB medium (pH 5.5) and in YNB medium adjusted to pH2.0. Genes involved in carbohydrate and amino acid metabolism, protein folding and stress response pathways were found to be differentially regulated in response to acidic environment in both the strains Agilent one-color experiment,Organism: Yeast ,Agilent-026378 Genotypic designed Custom Candida glabrata 8x15k , Labeling kit: Agilent Quick-Amp labeling
Project description:To examine the role of a glycosylphosphatidylinositol-linked aspartyl protease, CgYps1, in the regulation of pH homeostasis in Candida glabrata, transcriptional profiling analysis was carried out on wild-type and Cgyps1∆ cells grown in YNB medium (pH 5.5) and in YNB medium adjusted to pH 2.0. Genes involved in carbohydrate and amino acid metabolism, protein folding and stress response pathways were found to be differentially regulated in response to acidic environment in both the strains. To examine the role of a glycosylphosphatidylinositol-linked aspartyl protease, CgYps1, in the regulation of pH homeostasis in Candida glabrata, transcriptional profiling analysis was carried out on wild-type and Cgyps1∆ delta cells grown in YNB medium (pH 5.5) and in YNB medium adjusted to pH2.0. Genes involved in carbohydrate and amino acid metabolism, protein folding and stress response pathways were found to be differentially regulated in response to acidic environment in both the strains
