Mutant Versions of the S. cerevisiae Transcription Elongation Factor Spt16 Define Regions of Spt16 That Functionally Interact with Histone H3
| Autor: | Gary B. Berner, Kirby Martinez-Fonts, Megan N. Taylor, Sarah Alford, Catherine N. Myers, Andrea A. Duina, Jennifer Aileen Harper, Joseph H. Holthoff |
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| Rok vydání: | 2011 |
| Předmět: |
Genetic Screens
Saccharomyces cerevisiae Proteins Transcription Genetic DNA transcription lcsh:Medicine Yeast and Fungal Models RNA polymerase II Saccharomyces cerevisiae Transcription coregulator Chromatin remodeling Histones Molecular Genetics 03 medical and health sciences Model Organisms 0302 clinical medicine Genetics Histone code Gene Regulation lcsh:Science Biology RNA polymerase II holoenzyme 030304 developmental biology 0303 health sciences Multidisciplinary biology General transcription factor lcsh:R Eukaryotic transcription Chromatin Protein Structure Tertiary Cell biology Phenotype Mutation biology.protein lcsh:Q Mutant Proteins Gene expression Transcriptional Elongation Factors Transcription factor II D 030217 neurology & neurosurgery Protein Binding Research Article |
| Zdroj: | PLoS ONE PLoS ONE, Vol 6, Iss 6, p e20847 (2011) |
| ISSN: | 1932-6203 |
| DOI: | 10.1371/journal.pone.0020847 |
| Popis: | In eukaryotic cells, the highly conserved FACT (FAcilitates Chromatin Transcription) complex plays important roles in several chromatin-based processes including transcription initiation and elongation. During transcription elongation, the FACT complex interacts directly with nucleosomes to facilitate histone removal upon RNA polymerase II (Pol II) passage and assists in the reconstitution of nucleosomes following Pol II passage. Although the contribution of the FACT complex to the process of transcription elongation has been well established, the mechanisms that govern interactions between FACT and chromatin still remain to be fully elucidated. Using the budding yeast Saccharomyces cerevisiae as a model system, we provide evidence that the middle domain of the FACT subunit Spt16 – the Spt16-M domain – is involved in functional interactions with histone H3. Our results show that the Spt16-M domain plays a role in the prevention of cryptic intragenic transcription during transcription elongation and also suggest that the Spt16-M domain has a function in regulating dissociation of Spt16 from chromatin at the end of the transcription process. We also provide evidence for a role for the extreme carboxy terminus of Spt16 in functional interactions with histone H3. Taken together, our studies point to previously undescribed roles for the Spt16 M-domain and extreme carboxy terminus in regulating interactions between Spt16 and chromatin during the process of transcription elongation. |
| Databáze: | OpenAIRE |
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