ArticleMolecular and cellular biology2011
Domains of Tra1 important for activator recruitment and transcription coactivator functions of SAGA and NuA4 complexes.
Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
57 citing papers in PubMed, 91 citations in OpenAlex.
- Step-brothers in arms, SAGA and ATAC co-activator complexes, use different strategies.The EMBO journal · 2026Review
- Multi-Omics Dissection and Functional Validation of Candidate Regulators Modulating Stress Tolerance and Xylose Utilization in the Natural Yeast Strain YB-2625.Journal of fungi (Basel, Switzerland) · 2026Article
- A two-step regulatory mechanism dynamically controls histone H3 acetylation by SAGA complex at growth-related promoters.Nucleic acids research · 2025Article
- Novel Pathogenic Variant of theInternational journal of molecular sciences · 2025Article
- Article
- Inhibitors of phosphoinositide 3-kinase (PI3K) and phosphoinositide 3-kinase-related protein kinase family (PIKK).Journal of enzyme inhibition and medicinal chemistry · 2023Review
- The structure of the NuA4-Tip60 complex reveals the mechanism and importance of long-range chromatin modification.Nature structural & molecular biology · 2023Article
- Broad compatibility between yeast UAS elements and core promoters and identification of promoter elements that determine cofactor specificity.Cell reports · 2023Article
- Tra1 controls the transcriptional landscape of the aging cell.G3 (Bethesda, Md.) · 2023Article
- Genetic variation in P-element dysgenic sterility is associated with double-strand break repair and alternative splicing of TE transcripts.PLoS genetics · 2022Article
- Article
- An integrated SAGA and TFIID PIC assembly pathway selective for poised and induced promoters.Genes & development · 2022Article
- The TRRAP transcription cofactor represses interferon-stimulated genes in colorectal cancer cells.eLife · 2022Article
- Characterization of theJournal of fungi (Basel, Switzerland) · 2022Article
- TheFrontiers in microbiology · 2022Article
- The SAGA and NuA4 component Tra1 regulates Candida albicans drug resistance and pathogenesis.Genetics · 2021Article
- Mechanisms of stimulation of SAGA-mediated nucleosome acetylation by a transcriptional activator.Biochemistry and biophysics reports · 2021Article
- HAT cofactor TRRAP modulates microtubule dynamics via SP1 signaling to prevent neurodegeneration.eLife · 2021Article
- Transcription shapes genome-wide histone acetylation patterns.Nature communications · 2021Article
- The SAGA chromatin-modifying complex: the sum of its parts is greater than the whole.Genes & development · 2020Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The Tra1 protein is a direct transcription activator target that is essential for coactivator function of both the SAGA and NuA4 histone acetyltransferase (HAT) complexes. The ∼400-kDa Saccharomyces cerevisiae Tra1 polypeptide and its human counterpart TRRAP contain 67 or 68 tandem α-helical HEAT and TPR protein repeats that extend from the N terminus to the conserved yet catalytically inactive phosphatidylinositol 3-kinase (PI3K) domain. We generated a series of mutations spanning the length of the protein and assayed for defects in transcription, coactivator recruitment, and histone acetylation at SAGA- and NuA4-dependent genes. Inviable TRA1 mutants all showed defects in SAGA and NuA4 complex stability, suggesting that similar surfaces of Tra1 mediate assembly of these two very different coactivator complexes. Nearly all of the viable Tra1 mutants showed transcription defects that fell into one of three classes: (i) defective recruitment to promoters, (ii) reduced stability of the SAGA and NuA4 HAT modules, or (iii) normal recruitment of Tra1-associated subunits but reduced HAT activity in vivo. Our results show that Tra1 recruitment at Gcn4-dependent and Rap1-dependent promoters requires the same regions of Tra1 and that separate regions of Tra1 contribute to the HAT activity and stability of the SAGA and NuA4 HAT modules.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.