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Functional interaction between the transcription factor Sfp1 and the NuA4 complex in response to nutrient availability [CUT&RUN]

ABSTRACT: In this study, we investigate the physical and functional interaction between the transcription factor Sfp1 and the NuA4 complex in response to nutrient changes or stress. To study the functional interaction, we rapidly deplete Sfp1 or Esa1 (the catalytic subunit of NuA4) from nucleus, and performed CUT&RUN to profile all Sfp1/NuA4-regulated genes.

ORGANISM(S): Saccharomyces cerevisiae

PROVIDER: GSE267939 | GEO | 2026/05/01

REPOSITORIES: GEO

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Histone post-translational modification changes upon Sfp1 depletion

Project description:In this study, we investigate the physical and functional interaction between NuA4 and Sfp1. Sfp1 was rapidly depleted from yeast nuclei, and histone modification changes were detected by ChIP-sequencing.

2026-05-01 | GSE267779 | GEO

Functional interaction between the transcription factor Sfp1 and the NuA4 complex in response to nutrient availability[RNA]

Project description:Functional interaction between the transcription factor Sfp1 and the NuA4 complex in response to nutrient availability[RNA]

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Functional interaction between the transcription factor Sfp1 and the NuA4 complex in response to nutrient availability [CUT&RUN]

Project description:Functional interaction between the transcription factor Sfp1 and the NuA4 complex in response to nutrient availability [CUT&RUN]

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Functional interaction between the transcription factor Sfp1 and the NuA4 complex in response to nutrient availability[RNA]

Project description:In this study, we investigate gene expression profile upon carbon source shifts in yeast. RNA-sequencing was performed in Sfp1 wild-type strain and K655/657 mutants growing in different carbon sources.

2026-05-01 | GSE268202 | GEO

The NuA4 complex promotes Translesion Synthesis (TLS) - mediated DNA damage tolerance

Project description:DNA lesions can block a replication fork, leading to its collapse and gross chromosomal rearrangements. To circumvent such outcomes, DNA damage tolerance (DDT) pathways become engaged, allowing the replisome to bypass the lesion and complete S phase in the presence of unrepaired damage. Here we demonstrate a newly identified role for NuA4, including complex components Esa1 and Yng2, on the Translesion Synthesis (TLS) branch of DDT. Moreover, Our data suggest that NuA4 functionality within the tolerance pathway is likely direct as genome-wide transcriptional analysis with esa1-L254P mutants showed little changes in the expression of TLS factors compared to wild type during MMS treatment. When Yng2 expression is restricted to G2/M, cell viability and mutagenesis rates are restored to the levels measured when only the error-free branch of DDT is disrupted, indicating that the critical role of NuA4 in TLS functions in G2, after chromosomal replication is complete. Lastly, disruption of HTZ1, the Saccharomyces cerevisiae histone variant H2A.Z and target of NuA4, exhibits mutagenic rates of reversion that are comparable to the levels measured with NuA4 complex mutants, esa1-L254P and yng2M-NM-^T. The esa1-L254P strain was compared to wild type through a series of microarrays utilizing dye swaps with and without treatment of MMS. These included synchronized cells in G1 and S phase through alpha factor treatment. Four unique microarrays were performed each with dye swaps, comparing wild type to esa1-L254P in G1 and S phase with and without treatment with MMS. As a set of controls, four microarrays were performed comparing identical strains with and without MMS in G1 or S phase.

2015-02-21 | E-GEOD-66176 | biostudies-arrayexpress

Chromatin regulation by the NuA4 acetyltransferase complex is mediated by essential interactions between Enhancer of Polycomb (Epl1) and Esa1

Project description:Enzymes that modify and remodel chromatin are subunits in broadly conserved macromolecular complexes. One key chromatin modification is the dynamic acetylation of histones by opposing activities of acetyltransferase and deacetylase complexes. Among the acetyltransferases, the NuA4 complex containing Tip60 or its Saccharomyces cerevisiae ortholog, Esa1, is of particular significance because of its roles in crucial genomic processes including DNA damage repair and transcription. The catalytic subunit Esa1 is essential, as are five non-catalytic NuA4 subunits. We found that of these non-catalytic subunits, only deletion of Enhancer of polycomb (Epl1) can be bypassed by loss of a major deacetylase complex. This is a property shared by Esa1. Non-catalytic complex subunits are often critical for complex assembly, stability, genomic targeting, substrate specificity and regulation. Understanding the essential cellular role of Epl1 has been limited, a limitation now overcome by the discovery of its bypass suppression. Here, we present the first comprehensive in vivo study of Epl1 upon complete cellular loss of Epl1 using the powerful tool of suppression combined with transcriptional and mutational analyses. Our results highlight functional parallels between Epl1 and Esa1 and further illustrate that the structural role of Epl1 is important for promotion of Esa1 activity. This conclusion is strengthened by our dissection of Epl1 domains required in vivo for interaction with specific NuA4 subunits, histone acetylation, and chromatin targeting. These results provide new insights for the conserved, essential nature of Epl1 and its homologs among organisms, such as EPC1/2 in humans, which is frequently altered in cancers.

2017-01-19 | GSE92774 | GEO

The NuA4 complex promotes Translesion Synthesis (TLS) - mediated DNA damage tolerance

2015-02-21 | GSE66176 | GEO

NuA4 and H2A.Z control environmental responses and autotrophic growth in Arabidopsis

Project description:The nucleosomal acetyltransferase of H4 (NuA4) is an essential transcriptional coactivator in eukaryotes, though it remains poorly characterized in plants. Here, we describe Arabidopsis homologues of the NuA4 scaffold proteins Enhancer of Polycomb-Like1 (EPL1) and Esa1-Associated Factor1 (EAF1). Loss of AtEAF1 results in inhibition of growth and chloroplast development. These effects are stronger in the Atepl1 mutant and are further enhanced by loss of Golden2-Like (GLK) transcription factors suggesting that NuA4 activates nuclear plastidic genes alongside GLK. We demonstrate that AtEPL1 is necessary for nucleosomal acetylation of histones H4 and H2A.Z by NuA4 in vitro. These chromatin marks are diminished in Atepl1 genome-wide while another active chromatin mark H3K9ac is locally enhanced. Many chloroplast-related genes depend on NuA4 as they are downregulated with loss of H4ac and H2A.Z alone. Finally, we demonstrate that NuA4 promotes deposition of H2A.Z and by doing so prevents spurious activation of stress response genes.

2021-12-02 | GSE152940 | GEO

NuA4 and H2A.Z control environmental responses and autotrophic growth in Arabidopsis

Project description:Nucleosomal acetyltransferase of H4 (NuA4) is an essential transcriptional coactivator in eukaryotes, but remains poorly characterized in plants. Here, we describe Arabidopsis homologs of the NuA4 scaffold proteins Enhancer of Polycomb-Like-1 (AtEPL1) and Esa1- Associated Factor 1 (AtEAF1). Loss of AtEAF1 results in inhibition of growth and chloroplast development. These effects are stronger in the Atepl1 mutant and are further enhanced by loss of Golden2-Like (GLK) transcription factors, suggesting that NuA4 activates nuclear plastid genes alongside GLK. We demonstrate that AtEPL1 is necessary for nucleosomal acetylation of histones H4 and H2A.Z by NuA4 in vitro. These chromatin marks are diminished genome-wide in Atepl1, while another active chromatin mark, H3K9 acetylation (H3K9ac), is locally enhanced. Expression of many chloroplast-related genes depends on NuA4, as they are downregulated with loss of H4ac and H2A.Zac. Finally, we demonstrate that NuA4 promotes H2A.Z deposition and by doing so prevents spurious activation of stress response genes.

2021-12-20 | PXD030302 | Pride

SFP1 (ChIP-seq)

Project description:We set out to determine how Sfp1 binding targets evolved over time. We sampled our species of interest to include one pre-whole genome duplicaton (WGD) species containing SFP1A (K. lactis), one post-WGD species containing both SFP1 and SFP1PL (N. castellii), two post-WGD species containing only SFP1 (S. cerevisiae and S. paradoxus) and performed ChIP for each Sfp1 homolog in each species using an antibody that recognizes a conserved subdomain of Sfp1 common to both Sfp1, Sfp1a, and Sfp1pl. Because Sfp1pl was also present in N. castellii, a second antibody was used that is more specific to Sfp1pl (denoted as IP3). We also performed ChIP in SFP1 deletion mutants in each species tested, as a control."

2020-08-29 | GSE119211 | GEO

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