Forkhead proteins control the outcome of transcription factor binding by antiactivation
Autor: | Shinya Takahata, Jason D. Lieb, Yaxin Yu, Kelsi L. Kretschmann, Rebecca L. Parker, David J. Stillman, Warren P. Voth, Brett Milash |
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Rok vydání: | 2007 |
Předmět: |
TBX1
Chromatin Immunoprecipitation Saccharomyces cerevisiae Proteins Response element Plasma protein binding Saccharomyces cerevisiae Biology DNA-binding protein General Biochemistry Genetics and Molecular Biology Article Fungal Proteins Histones Open Reading Frames Forkhead Transcription Factors Gene Expression Regulation Fungal Promoter Regions Genetic Molecular Biology Transcription factor General Immunology and Microbiology General Neuroscience Cell Cycle Acetylation DNA Molecular biology Cell biology Protein Structure Tertiary DNA-Binding Proteins Histone deacetylase complex Chromatin immunoprecipitation hormones hormone substitutes and hormone antagonists Protein Binding Transcription Factors |
Zdroj: | The EMBO journal. 26(20) |
ISSN: | 1460-2075 |
Popis: | Transcription factors with identical DNA‐binding specificity often activate different genes in vivo . Yeast Ace2 and Swi5 are such activators, with targets we classify as Swi5‐only, Ace2‐only, or both. We define two unique regulatory modes. Ace2 and Swi5 both bind in vitro to Swi5‐only genes such as HO , but only Swi5 binds and activates in vivo . In contrast, Ace2 and Swi5 both bind in vivo to Ace2‐only genes, such as CTS1 , but promoter‐bound Swi5 fails to activate. We show that activation by Swi5 is prevented by the binding of the Forkhead factors Fkh1 and Fkh2, which recruit the Rpd3(Large) histone deacetylase complex to the CTS1 promoter. Global analysis shows that all Ace2‐only genes are bound by both Ace2 and Swi5, and also by Fkh1/2. Genes normally activated by either Ace2 or Swi5 can be converted to Ace2‐only genes by the insertion of Fkh‐binding sites. Thus Fkh proteins, which function initially to activate SWI5 and ACE2 , subsequently function as Swi5‐specific antiactivators. |
Databáze: | OpenAIRE |
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