ArticlePloS one2011
Mutant versions of the S. cerevisiae transcription elongation factor Spt16 define regions of Spt16 that functionally interact with histone H3.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 28 citations in OpenAlex.
- A histone H2A docking domain mutant interferes with proper yFACT-gene interactions inmicroPublication biology · 2026Article
- Gene editing and CRISPR-dependent homology-mediated end joining.Experimental & molecular medicine · 2025Review
- Assessing contributions of DNA sequences at the 3' end of a yeast gene on yFACT, RNA polymerase II, and nucleosome occupancy.BMC research notes · 2024Article
- Pluripotency state transition of embryonic stem cells requires the turnover of histone chaperone FACT on chromatin.iScience · 2024Article
- Trapping of yFACT at 3' ends of genes is not a universal characteristic of yeast versions of Bryant-Li-Bhoj syndrome histone H3 mutants.microPublication biology · 2024Article
- Dominant effects of the histone mutant H3-L61R on Spt16-gene interactions in budding yeast.Epigenetics · 2022Article
- Prevention of Chromatin Destabilization by FACT Is Crucial for Malignant Transformation.iScience · 2020Article
- Structure and function of the histone chaperone FACT - Resolving FACTual issues.Biochimica et biophysica acta. Gene regulatory mechanisms · 2018Review
- Charged residues on the side of the nucleosome contribute to normal Spt16-gene interactions in budding yeast.Epigenetics · 2018Article
- Integrated molecular mechanism directing nucleosome reorganization by human FACT.Genes & development · 2016Article
- Structure of the human histone chaperone FACT Spt16 N-terminal domain.Acta crystallographica. Section F, Structural biology communications · 2016Article
- A systematic mutational analysis of a histone H3 residue in budding yeast provides insights into chromatin dynamics.G3 (Bethesda, Md.) · 2015Article
- A nucleosomal region important for ensuring proper interactions between the transcription elongation factor Spt16 and transcribed genes in Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2013Article
- Histone chaperone FACT action during transcription through chromatin by RNA polymerase II.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Structure of the Spt16 middle domain reveals functional features of the histone chaperone FACT.The Journal of biological chemistry · 2013Article
- Identification of Mutant Versions of the Spt16 Histone Chaperone That Are Defective for Transcription-Coupled Nucleosome Occupancy in Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2012Article
- The role of FACT in making and breaking nucleosomes.Biochimica et biophysica acta · 2012Article
- Article
- Histone Chaperones Spt6 and FACT: Similarities and Differences in Modes of Action at Transcribed Genes.Genetics research international · 2011Article
- Regulation of chromatin structure and function: insights into the histone chaperone FACT.Cell cycle (Georgetown, Tex.)Review
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
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.
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