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BET family members Bdf1/2 modulate global transcription initiation and elongation in Saccharomyces cerevisiae

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Saccharomyces cerevisiae

PROVIDER: GSE171067 | GEO | 2021/06/09

REPOSITORIES: GEO

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BET family members Bdf1/2 modulate global transcription initiation and elongation in Saccharomyces cerevisiae.

Project description:Human bromodomain and extra-terminal domain (BET) family members are promising targets for therapy of cancer and immunoinflammatory diseases, but their mechanisms of action and functional redundancies are poorly understood. Bdf1/2, yeast homologues of the human BET factors, were previously proposed to target transcription factor TFIID to acetylated histone H4, analogous to bromodomains that are present within the largest subunit of metazoan TFIID. We investigated the genome-wide roles of Bdf1/2 and found that their important contributions to transcription extend beyond TFIID function as transcription of many genes is more sensitive to Bdf1/2 than to TFIID depletion. Bdf1/2 co-occupy the majority of yeast promoters and affect preinitiation complex formation through recruitment of TFIID, Mediator, and basal transcription factors to chromatin. Surprisingly, we discovered that hypersensitivity of genes to Bdf1/2 depletion results from combined defects in transcription initiation and early elongation, a striking functional similarity to human BET proteins, most notably Brd4. Our results establish Bdf1/2 as critical for yeast transcription and provide important mechanistic insights into the function of BET proteins in all eukaryotes.

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BET family members Bdf1/2 modulate global transcription initiation and elongation in Saccharomyces cerevisiae (RNA-Seq)

Project description:Human BET family members are promising targets in the therapy of cancer and immunoinflammatory diseases, but their mechanism of action and functional redundancies are poorly understood. Yeast BET factors Bdf1/2 were previously proposed to act as anchors for coactivator TFIID. We investigated their genome wide roles in transcription and found that, while they cooperate with TFIID at many genes, their contributions to transcription are often significantly different. Bdf1/2 co-occupy the majority of yeast promoters and affect preinitiation complex formation by participating in recruitment of TFIID, Mediator and basal factors to chromatin. Surprisingly, we discovered that hypersensitivity of genes to Bdf1/2 depletion results from combined defects in initiation of transcription and early elongation. Bdf1/2 are critical components of yeast transcriptional machinery with many functional similarities to human BET proteins, most notably Brd4.

2021-06-09 | GSE171065 | GEO

BET family members Bdf1/2 modulate global transcription initiation and elongation in Saccharomyces cerevisiae (ChIP-Seq)

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BET family members Bdf1/2 modulate global transcription initiation and elongation in Saccharomyces cerevisiae (ChEC-Seq)

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BET family members Bdf1/2 modulate global transcription initiation and elongation in Saccharomyces cerevisiae

Project description:BET family members Bdf1/2 modulate global transcription initiation and elongation in Saccharomyces cerevisiae

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BET family members Bdf1/2 modulate global transcription initiation and elongation in Saccharomyces cerevisiae (ChEC-Seq)

Project description:BET family members Bdf1/2 modulate global transcription initiation and elongation in Saccharomyces cerevisiae (ChEC-Seq)

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BET family members Bdf1/2 modulate global transcription initiation and elongation in Saccharomyces cerevisiae (ChIP-Seq)

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BET family members Bdf1/2 modulate global transcription initiation and elongation in Saccharomyces cerevisiae (RNA-Seq)

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Role of the uS9/yS16 C-terminal tail in translation initiation and elongation in Saccharomyces cerevisiae.

Project description:The small ribosomal subunit protein uS9 (formerly called rpS16 in Saccharomyces cerevisiae), has a long protruding C-terminal tail (CTT) that extends towards the mRNA cleft of the ribosome. The last C-terminal residue of uS9 is an invariably conserved, positively charged Arg that is believed to enhance interaction of the negatively charged initiator tRNA with the ribosome when the tRNA is base-paired to the AUG codon in the P-site. In order to more fully characterize the role of the uS9 CTT in eukaryotic translation, we tested how truncations, extensions and substitutions within the CTT affect initiation and elongation processes in Saccharomyces cerevisiae. We found that uS9 C-terminal residues are critical for efficient recruitment of the eIF2•GTP•Met-tRNAiMet ternary complex to the ribosome and for its proper response to the presence of an AUG codon in the P-site during the scanning phase of initiation. These residues also regulate hydrolysis of the GTP in the eIF2•GTP•Met-tRNAiMet complex to GDP and Pi. In addition, our data show that uS9 CTT modulates elongation fidelity. Therefore, we propose that uS9 CTT is critical for proper control of the complex interplay of events surrounding accommodation of initiator and elongator tRNAs in the P- and A-sites of the ribosome.

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