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Prp5-Spt8/Spt3 Interaction Mediates a Reciprocal Coupling between Splicing and Transcription

ABSTRACT: Prp5-Spt8/Spt3 Interaction Mediates a Reciprocal Coupling between Splicing and Transcription

PROVIDER: PRJNA613270 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR11458943_1.fastq.gz	Fastqsanger.gz
	SRR11458943_2.fastq.gz	Fastqsanger.gz
	SRR11458944_1.fastq.gz	Fastqsanger.gz
	SRR11458944_2.fastq.gz	Fastqsanger.gz
	SRR11458945_1.fastq.gz	Fastqsanger.gz

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Prp5-Spt8/Spt3 interaction mediates a reciprocal coupling between splicing and transcription.

Project description:Transcription and pre-mRNA splicing are coupled to promote gene expression and regulation. However, mechanisms by which transcription and splicing influence each other are still under investigation. The ATPase Prp5p is required for pre-spliceosome assembly and splicing proofreading at the branch-point region. From an open UV mutagenesis screen for genetic suppressors of prp5 defects and subsequent targeted testing, we identify components of the TBP-binding module of the Spt-Ada-Gcn5 Acetyltransferase (SAGA) complex, Spt8p and Spt3p. Spt8Δ and spt3Δ rescue the cold-sensitivity of prp5-GAR allele, and prp5 mutants restore growth of spt8Δ and spt3Δ strains on 6-azauracil. By chromatin immunoprecipitation (ChIP), we find that prp5 alleles decrease recruitment of RNA polymerase II (Pol II) to an intron-containing gene, which is rescued by spt8Δ. Further ChIP-seq reveals that global effects on Pol II-binding are mutually rescued by prp5-GAR and spt8Δ. Inhibited splicing caused by prp5-GAR is also restored by spt8Δ. In vitro assays indicate that Prp5p directly interacts with Spt8p, but not Spt3p. We demonstrate that Prp5p's splicing proofreading is modulated by Spt8p and Spt3p. Therefore, this study reveals that interactions between the TBP-binding module of SAGA and the spliceosomal ATPase Prp5p mediate a balance between transcription initiation/elongation and pre-spliceosome assembly.

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Spt3 and Spt8 are involved in the formation of a silencing boundary by interacting with TATA-binding protein

Project description:In Saccharomyces cerevisiae, a heterochromatin-like chromatin structure called the silencing region is present at the telomere as a complex of Sir2, Sir3, and Sir4. Sir2 is a histone deacetylase, and Sir3 and Sir4 promote spreading of the silencing region at the telomere. Histone acetyltransferases restrict the silencing region. Here, we show that Spt3 and Spt8 block the spread of silencing regions. Spt3 and Spt8 are members of the Spt-Ada-Gcn5-acetyltransferase (SAGA) complex, which has histone acetyltransferase activity. Although both Spt3 and Spt8 interact with telomere-binding proteins (TBPs), Spt3 had a greater effect on genome-wide transcription. Mutant analysis showed that TBPs play an important role in boundary formation, in particular the interaction between Spt3 and TBPs.

2023-03-29 | GSE220290 | GEO

Prp5-Spt8/Spt3 Interaction Mediates a Reciprocal Coupling between Splicing and Transcription

Project description:Transcription and pre-mRNA splicing are coupled to promote gene expression and regulation. However, mechanisms by which transcription and splicing influence each other are still under investigation. The ATPase Prp5p is required for pre-spliceosome assembly and splicing proofreading at the branch-point region. From an open UV mutagenesis screen for genetic suppressors of prp5 defects and subsequent targeted testing, we identify components of the TBP-binding module of the Spt–Ada–Gcn5 Acetyltransferase (SAGA) complex, Spt8p and Spt3p. Spt8Δ and spt3Δ rescue the cold-sensitivity of prp5-GAR allele, and prp5 mutants restore growth of spt8Δ and spt3Δ strains on 6-azauracil. By chromatin immunoprecipitation (ChIP), we find that prp5 alleles decrease recruitment of RNA polymerase II (Pol II) to an intron-containing gene, which is rescued by spt8Δ. Further ChIP-seq reveals that global effects on Pol II-binding is mutually rescued by prp5 mutant and spt8Δ. Inhibited splicing caused by prp5-GAR is also restored by spt8Δ. In vitro assay indicates that Prp5p directly interacts with Spt8p, but not Spt3p. We demonstrate that Prp5p’s splicing proofreading is modulated by Spt8p and Spt3p. Therefore, this study reveals that interactions between the TBP-binding module of SAGA and the spliceosomal ATPase Prp5p mediate a balance between transcription initiation/elongation and pre-spliceosome assembly.

2020-04-17 | GSE147179 | GEO

Coactivator SAGA plays a crucial role in TBP recruitment for the Gcn4 transcriptome via subunits Spt3/Spt8 [RNA-seq]

Project description:Transcription initiation by RNA polymerase II is facilitated by coactivators that recruit general initiation factors to promoters. Coactivator complexes TFIID and SAGA recruit TATA-binding protein (TBP), while SAGA also enhances transcription by histone acetylation via the HAT Gcn5. It was proposed that most yeast genes depend exclusively on TFIID, with only ~10% requiring cumulative contributions by SAGA and TFIID for efficient transcription. It was further suggested that genes induced by Gcn4, transcriptional activator of amino acid biosynthetic genes induced by amino acid starvation, depend on the HAT but not the TBP-recruitment function of SAGA. At odds with this model, ChIP-sequencing of TBP and Pol II subunit Rpb1 revealed that deleting SPT3 or SPT8, but not GCN5, reduced TBP binding at many Gcn4 target genes. In contrast, deleting GCN5 but not SPT3 or SPT8 impaired promoter histone eviction at the highly remodeled subset of induced genes, whereas transcription was broadly reduced by all three SAGA mutations. Nuclear depletion of TFIID subunit Taf1 generally reduced TBP recruitment at these and most other SAGA-dependent genes only in cells lacking Spt3 or Spt8. We conclude that SAGA is crucial for TBP recruitment via Spt3/Spt8, beyond its role in histone acetylation, and functions non-redundantly with TFIID in the Gcn4 transcriptome of amino acid-starved cells.

2025-07-16 | GSE295279 | GEO

Coactivator SAGA plays a crucial role in TBP recruitment for the Gcn4 transcriptome via subunits Spt3/Spt8

Project description:Coactivator complexes TFIID and SAGA recruit TATA-binding protein (TBP), while SAGA also enhances transcription by histone acetylation via the HAT Gcn5. It was proposed that most yeast genes depend exclusively on TFIID, with only ~10% requiring cumulative contributions by SAGA and TFIID for efficient transcription. It was further suggested that genes induced by Gcn4, transcriptional activator of amino acid biosynthetic genes induced by amino acid starvation, depend on the HAT, but not TBP-recruitment function of SAGA. At odds with this model, ChIP-sequencing of TBP and Pol II subunit Rpb1 revealed that deleting SPT3 or SPT8, but not GCN5, reduced TBP binding at most Gcn4 target genes, whereas deleting GCN5 selectively impaired promoter histone eviction; and all three SAGA mutations reduced transcription comparably. Nuclear depletion of TFIID subunit Taf1 generally reduced TBP recruitment at these and most other SAGA-dependent genes only in cells lacking Spt3 or Spt8. We conclude that SAGA is crucial for TBP recruitment via Spt3/Spt8, beyond its role in histone acetylation, whereas TFIID plays an ancillary role for the Gcn4 transcriptome in amino acid-starved cells.

2025-07-16 | GSE280732 | GEO

Cardiomyocyte-specific ADGRF5 mediates cardiac homeostasis via Gαq coupling

Project description:Cardiomyocyte-specific ADGRF5 mediates cardiac homeostasis via Gαq coupling

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NOTCH1 mediates a reciprocal switch between two distinct secretomes during senescence

Project description:NOTCH1 mediates a reciprocal switch between two distinct secretomes during senescence

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Transcription profiling of S. cerevisiae wild type reference strain, two simple mutants (not1-2 and spt3) and one double mutant (not1-2 spt3) reveals a SAGA-Independent function of SPT3 mediates transcriptional deregulation in a mutant of the Ccr4-Not Complex

Project description:The conserved multi-subunit Ccr4-Not complex regulates gene expression in diverse ways. In this work, we characterize the suppression of temperature sensitivity associated with a mutation in the gene encoding the scaffold subunit of the Ccr4-Not complex, NOT1, by the deletion of SPT3. We determine that the deletion of SPT3, but not the deletion of genes encoding other subunits of the SAGA complex, globally suppresses transcriptional defects of not1-2. We find that transcriptional activation in not1-2 is associated with increased binding of TFIID and SAGA at promoters of upregulated genes, and this is suppressed by the deletion of SPT3. Interestingly, Spt3p-dependent activation of transcription occurs in not1-2 even if the SAGA complex is disrupted by the deletion of SPT7 that encodes a subunit of SAGA required for its integrity. Consistent with a SAGA-independent function of Spt3p, the deletion of SPT3 displays synthetic phenotypes when combined with a deletion of SPT7. Taken together, our results provide a new view of the Spt3 protein by identifying a SAGA-independent function of this protein that is functionally linked to the Ccr4-Not complex. Experiment Overall Design: 4 strains were analyzed: the wild type reference strain, two simple mutants (not1-2 and spt3) and one double mutant (not1-2 spt3). All strains were in duplicate.

2008-06-16 | E-GEOD-9432 | biostudies-arrayexpress

Hypoxia-induced CTCF mediates alternative splicing via coupling chromatin looping and RNA Pol II pause to promote EMT in breast cancer

Project description:Hypoxia-induced CTCF mediates alternative splicing via coupling chromatin looping and RNA Pol II pause to promote EMT in breast cancer

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A SAGA-Independent Function of SPT3 Mediates Transcriptional Deregulation in a Mutant of the Ccr4-Not Complex

2007-10-26 | GSE9432 | GEO