ArticleGenetics2007
Characterization of new Spt3 and TATA-binding protein mutants of Saccharomyces cerevisiae: Spt3 TBP allele-specific interactions and bypass of Spt8.
Article in Genetics, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 44 citations in OpenAlex.
- Spt3 and Spt8 Are Involved in the Formation of a Silencing Boundary by Interacting with TATA-Binding Protein.Biomolecules · 2023Article
- SUPT3H-less SAGA coactivator can assemble and function without significantly perturbing RNA polymerase II transcription in mammalian cells.Nucleic acids research · 2022Article
- Genome-Wide Regulations of the Preinitiation Complex Formation and Elongating RNA Polymerase II by an E3 Ubiquitin Ligase, San1.Molecular and cellular biology · 2022Article
- TheFrontiers in microbiology · 2022Article
- The biochemical and genetic discovery of the SAGA complex.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021Review
- The SAGA continues: The rise of cis- and trans-histone crosstalk pathways.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021Review
- The SAGA chromatin-modifying complex: the sum of its parts is greater than the whole.Genes & development · 2020Review
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- A synthetic non-histone substrate to study substrate targeting by the Gcn5 HAT and sirtuin HDACs.The Journal of biological chemistry · 2019Article
- Distinct requirements of linker DNA and transcriptional activators in promoting SAGA-mediated nucleosome acetylation.The Journal of biological chemistry · 2018Article
- Mechanistic Differences in Transcription Initiation at TATA-Less and TATA-Containing Promoters.Molecular and cellular biology · 2018Article
- SAGA Is a General Cofactor for RNA Polymerase II Transcription.Molecular cell · 2017Article
- Coactivators and general transcription factors have two distinct dynamic populations dependent on transcription.The EMBO journal · 2017Article
- The Spliceosomal Protein SF3B5 is a Novel Component of Drosophila SAGA that Functions in Gene Expression Independent of Splicing.Journal of molecular biology · 2016Article
- SGF29 and Sry pathway in hepatocarcinogenesis.World journal of biological chemistry · 2015Review
- Architecture of the Saccharomyces cerevisiae SAGA transcription coactivator complex.The EMBO journal · 2014Article
- Mutations on the DNA binding surface of TBP discriminate between yeast TATA and TATA-less gene transcription.Molecular and cellular biology · 2014Article
- Dancing the cell cycle two-step: regulation of yeast G1-cell-cycle genes by chromatin structure.Trends in biochemical sciences · 2013Review
- SAGA function in tissue-specific gene expression.Trends in cell biology · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The Spt-Ada-Gcn5-acetyltransferase (SAGA) complex of Saccharomyces cerevisiae is a multifunctional coactivator complex that has been shown to regulate transcription by distinct mechanisms. Previous results have shown that the Spt3 and Spt8 components of SAGA regulate initiation of transcription of particular genes by controlling the level of TATA-binding protein (TBP/Spt15) associated with the TATA box. While biochemical evidence exists for direct Spt8-TBP interactions, similar evidence for Spt3-TBP interactions has been lacking. To learn more about Spt3-TBP interactions in vivo, we have isolated a new class of spt3 mutations that cause a dominant-negative phenotype when overexpressed. These mutations all cluster within a conserved region of Spt3. The isolation of extragenic suppressors of one of these spt3 mutations has identified two new spt15 mutations that show allele-specific interactions with spt3 mutations with respect to transcription and the recruitment of TBP to particular promoters. In addition, these new spt15 mutations partially bypass an spt8 null mutation. Finally, we have examined the level of SAGA-TBP physical interaction in these mutants. While most spt3, spt8, and spt15 mutations do not alter SAGA-TBP interactions, one spt3 mutation, spt3-401, causes a greatly increased level of SAGA-TBP physical association. These results, taken together, suggest that a direct Spt3-TBP interaction is required for normal TBP levels at Spt3-dependent promoters in vivo.
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Registered trials
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.