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The Candida albicans Histone Acetyltransferase Hat1 Regulates Stress Resistance and Virulence via Distinct Chromatin Assembly Pathways

ABSTRACT: Transcriptome analysis of wild type, Hat1-deficient, Cac2-deficient and Rtt109-deficient Candida albicans cells prior to and after treatment with hydrogen was done to determine the transcriptional changes in these three mutatns in logarithmically growing cells as well as under oxidative stress conditions.

ORGANISM(S): Candida albicans

PROVIDER: GSE73409 | GEO | 2015/09/25

SECONDARY ACCESSION(S): PRJNA296914

REPOSITORIES: GEO

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The Candida albicans Histone Acetyltransferase Hat1 Regulates Stress Resistance and Virulence via Distinct Chromatin Assembly Pathways.

Project description:Human fungal pathogens like Candida albicans respond to host immune surveillance by rapidly adapting their transcriptional programs. Chromatin assembly factors are involved in the regulation of stress genes by modulating the histone density at these loci. Here, we report a novel role for the chromatin assembly-associated histone acetyltransferase complex NuB4 in regulating oxidative stress resistance, antifungal drug tolerance and virulence in C. albicans. Strikingly, depletion of the NuB4 catalytic subunit, the histone acetyltransferase Hat1, markedly increases resistance to oxidative stress and tolerance to azole antifungals. Hydrogen peroxide resistance in cells lacking Hat1 results from higher induction rates of oxidative stress gene expression, accompanied by reduced histone density as well as subsequent increased RNA polymerase recruitment. Furthermore, hat1Δ/Δ cells, despite showing growth defects in vitro, display reduced susceptibility to reactive oxygen-mediated killing by innate immune cells. Thus, clearance from infected mice is delayed although cells lacking Hat1 are severely compromised in killing the host. Interestingly, increased oxidative stress resistance and azole tolerance are phenocopied by the loss of histone chaperone complexes CAF-1 and HIR, respectively, suggesting a central role for NuB4 in the delivery of histones destined for chromatin assembly via distinct pathways. Remarkably, the oxidative stress phenotype of hat1Δ/Δ cells is a species-specific trait only found in C. albicans and members of the CTG clade. The reduced azole susceptibility appears to be conserved in a wider range of fungi. Thus, our work demonstrates how highly conserved chromatin assembly pathways can acquire new functions in pathogenic fungi during coevolution with the host.

| S-EPMC4608838 | biostudies-literature

Hat1 WT and Hat1 KO MEFs analyzed to identify sites of acetylation that are dependent on Hat1

Project description:Hat1 WT and Hat1 KO MEFs were grown on both galactose and glucose. Abundance of acetylated peptides was compared between the samples.

2020-02-28 | PXD017362 | Pride

HAT1 coordinates histone production and acetylation via H4 promoter binding

Project description:The energetic costs of duplicating chromatin are large and therefore likely depend on nutrient sensing checkpoints and metabolic inputs. By studying chromatin modifiers regulated by epithelial growth factor, we identified histone acetyltransferase 1 (HAT1) as an induced gene that enhances proliferation through coordinating histone production, acetylation and glucose metabolism. In addition to its canonical role as a cytoplasmic histone H4 acetyltransferase, we isolated a HAT1-containing complex bound specifically at promoters of H4 genes. HAT1-dependent transcription of H4 genes required an acetate-sensitive promoter element. HAT1 expression was critical for S-phase progression and maintenance of H3 lysine 9 acetylation at proliferation-associated genes, including histone genes. Therefore, these data describe a feed-forward circuit whereby HAT1 captures acetyl-groups on nascent histones and drives H4 production by chromatin binding to support chromatin replication and acetylation. These findings have important implications for human disease, since high HAT1 levels associate with poor outcomes across multiple cancer types.

2019-07-02 | GSE117472 | GEO

Transcription factor AmyR and Molecular brake Hat1 modulate amylase gene expression in Penicillium oxalicum

Project description:The goals of this study are to compare different gene expressions for Penicillium oxalicum wild type strain (WT), Hat1 deletion strain (ΔHat1) and AmyR deletion strain (ΔAmyR) in 2% starch as carbon sources. The correlation analysis results between the various samples showed that the gene expression levels of the wild strain and the ΔHat1 strain were significantly different, and the gene expression levels between ΔAmyR and the wild strain were also significantly different. The deletion of Hat1 significantly up-regulates the expression levels of amylase genes of Penicillium oxalicum, and the absence of AmyR can significantly down-regulate the expression level of amylase genes genes, indicating that Hat1 and AmyR can cause a difference in amylase synthesis by affecting the expression of amylase genes. The information provided by this study indicates that Hat1 and AmyR functions are necessary for the amylase activity of Penicillium oxalicum.

2021-05-28 | GSE175682 | GEO

RNA-seq datasets of Trypanosoma brucei WT cells and 2T1 cells, which were depleted of HAT1 or HAT2 for 48 h

Project description:To analyze the effect of HAT1 or HAT2 depletion on transcript levels, we performed RNA-seq analyses comparing the transcript levels after 48 h of HAT1 or HAT2 depletion to WT levels.

2020-02-21 | GSE145622 | GEO

RNA abundance in wild-type and rtt109 -/- Candida albicans, with and without peroxide stress

2010-01-04 | GSE18936 | GEO

Epigenetic Regulation of Nuclear Lamina-Associated Heterochromatin by HAT1 and the Acetylation of Newly Synthesized Histones [pMEF_ATAC_Seq]

Project description:We report that HAT1 regulates chromatin accessibility of large chromosomal domains.

2021-12-01 | GSE178590 | GEO

Epigenetic Regulation of Nuclear Lamina-Associated Heterochromatin by HAT1 and the Acetylation of Newly Synthesized Histones [imMEF_ATAC_Seq]

Project description:We report that HAT1 regulates chromatin accessibility of large chromosomal domains.

2021-12-01 | GSE178589 | GEO

A novel role for the histone acetyltransferase Hat1 in the CENP-A/CID assembly pathway in Drosophila melanogaster.

Project description:The incorporation of CENP-A into centromeric chromatin is an essential prerequisite for kinetochore formation. Yet, the molecular mechanisms governing this process are surprisingly divergent in different organisms. While CENP-A loading mechanisms have been studied in some detail in mammals, there are still large gaps to our understanding of CENP-A/Cid loading pathways in Drosophila. Here, we report on the characterization and delineation of at least three different CENP-A preloading complexes in Drosophila. Two complexes contain the CENP-A chaperones CAL1, FACT and/or Caf1/Rbap48. Notably, we identified a novel complex consisting of the histone acetyltransferase Hat1, Caf1 and CENP-A/H4. We show that Hat1 is required for proper CENP-A loading into chromatin, since knock-down in S2 cells leads to reduced incorporation of newly synthesized CENP-A. In addition, we demonstrate that CENP-A/Cid interacts with the HAT1 complex via an N-terminal region, which is acetylated in cytoplasmic but not in nuclear CENP-A. Since Hat1 is not responsible for acetylation of CENP-A/Cid, these results suggest a histone acetyltransferase activity-independent escort function for Hat1. Thus, our results point toward intriguing analogies between the complex processing pathways of newly synthesized CENP-A and canonical histones.

| S-EPMC4797270 | biostudies-literature

RNA abundance in wild-type and rtt109 -/- Candida albicans, with and without peroxide stress

Project description:Candida albicans is a ubiquitous opportunistic pathogen that is the most prevalent cause of hospital-acquired fungal infections. In mammalian hosts, C. albicans is engulfed by phagocytes that attack the pathogen with DNA-damaging reactive oxygen species (ROS). Acetylation of histone H3 lysine 56 (H3K56) by the fungal-specific histone acetyltransferase Rtt109 is important for yeast model organisms to survive DNA damage and maintain genome integrity. To assess the importance of Rtt109 for C. albicans pathogenicity, we deleted the predicted homologue of Rtt109 in the clinical C. albicans isolate, SC5314. C. albicans rtt109 -/- mutant cells lack acetylated H3K56 (H3K56ac) and are hypersensitive to genotoxic agents. Additionally, rtt109 -/- mutant cells constitutively display increased H2A S129 phosphorylation and elevated DNA repair gene expression, consistent with endogenous DNA damage. Four independent pairs of biological replicate samples were analyzed to compare RNA levels in wild-type and rtt109 -/- cells. Two experiments were performed: first, in unperturbed cells grown in YPD and second, in cells exposed to H2O2. To account for dye effects, two of the four samples for each experiment were analyzed using Cy3 labeling of the wild-type sample and Cy5 labeling of the mutant sample; the dyes were swapped for the other two biological replicates.

2010-05-16 | E-GEOD-18936 | biostudies-arrayexpress

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