ArticleBiochemistry2012
Sgf29p facilitates the recruitment of TATA box binding protein but does not alter SAGA's global structural integrity in vivo.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 21 citations in OpenAlex.
- Structure of the transcriptional co-activator SAGA complex, including the histone acetyltransferase module.Molecular cell · 2025Article
- Chromatin and non-chromatin immunoprecipitations to capture protein-protein and protein-nucleic acid interactions in living cells.Methods (San Diego, Calif.) · 2023Article
- Article
- The SAGA HAT module is tethered by its SWIRM domain and modulates activity of the SAGA DUB module.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023Article
- TheFrontiers in microbiology · 2022Article
- The biochemical and genetic discovery of the SAGA complex.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021Review
- Mechanisms of Antisense Transcription Initiation with Implications in Gene Expression, Genomic Integrity and Disease Pathogenesis.Non-coding RNA · 2019Review
- Two Distinct Regulatory Mechanisms of Transcriptional Initiation in Response to Nutrient Signaling.Genetics · 2018Article
- Convergent microevolution of Cryptococcus neoformans hypervirulence in the laboratory and the clinic.Scientific reports · 2017Article
- Nucleosome competition reveals processive acetylation by the SAGA HAT module.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- SGF29 and Sry pathway in hepatocarcinogenesis.World journal of biological chemistry · 2015Review
- Composition of the SAGA complex in plants and its role in controlling gene expression in response to abiotic stresses.Frontiers in plant science · 2015Review
- Sus1p facilitates pre-initiation complex formation at the SAGA-regulated genes independently of histone H2B de-ubiquitylation.Journal of molecular biology · 2014Article
- Cell-cycle perturbations suppress the slow-growth defect of spt10Δ mutants in Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2013Article
- Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Although Sgf29p has been biochemically implicated as a component of SAGA (Spt-Ada-Gcn5 acetyltransferase), its precise mechanism of action in transcription is not clearly understood in vivo. Here, using a formaldehyde-based in vivo cross-linking and chromatin immunoprecipitation (ChIP) assay in conjunction with transcriptional and mutational analyses, we show that Sgf29p along with other SAGA components is recruited to the upstream activating sequence (UAS) of a SAGA-regulated gene, GAL1, in an activation domain-dependent manner. However, Sgf29p does not alter the recruitment of Spt20p that maintains the overall structural and functional integrity of SAGA. The recruitment of other SAGA components such as TAF10p, TAF12p, and Ubp8p to the GAL1 UAS is also not altered in the absence of Sgf29p. Interestingly, we find that the recruitment of TBP (TATA box binding protein that nucleates the assembly of general transcription factors to form the preinitiation complex for transcriptional initiation) to the core promoter of GAL1 is weakened in Δsgf29. Likewise, Sgf29p also enhances the recruitment of TBP to other SAGA-regulated promoters. Such weakening of recruitment of TBP to these promoters subsequently decreases the level of transcription. Taken together, these results support the idea that SAGA-associated Sgf29p facilitates the recruitment of TBP (and hence transcription) without altering the global structural integrity of SAGA in vivo.
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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.