ArticleNucleic acids research2017
The elongation factor Spt4/5 regulates RNA polymerase II transcription through the nucleosome.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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44 citing papers in PubMed, 74 citations in OpenAlex.
- Spt5's central KOW domains and the Pol II stalk collaborate to regulate chromatin and 3'-end processing in Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2026Article
- Structural basis of transcription-coupled H3K36 trimethylation by Set2 in coordination with FACT.Science advances · 2026Article
- The histone chaperone Spt6 controls chromatin structure through its conserved N-terminal domain.Molecular cell · 2025Article
- FACT weakens the nucleosomal barrier to transcription and preserves its integrity by forming a hexasome-like intermediate.Molecular cell · 2025Article
- Multiple structures of RNA polymerase II isolated from human nuclei by ChIP-CryoEM analysis.Nature communications · 2025Article
- A function of TPL/TBL1-type corepressors is to nucleate the assembly of the preinitiation complex.The Journal of cell biology · 2025Article
- Single-molecule imaging for investigating the transcriptional control.Molecules and cells · 2025Review
- NusG-Spt5 Transcription Factors: Universal, Dynamic Modulators of Gene Expression.Journal of molecular biology · 2025Review
- A conserved function of corepressors is to nucleate assembly of the transcriptional preinitiation complex.bioRxiv : the preprint server for biology · 2024Article
- Elf1 promotes Rad26's interaction with lesion-arrested Pol II for transcription-coupled repair.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Binding of small molecule inhibitors to RNA polymerase-Spt5 complex impacts RNA and DNA stability.Journal of computer-aided molecular design · 2023Article
- Insights into Spt6: a histone chaperone that functions in transcription, DNA replication, and genome stability.Trends in genetics : TIG · 2023Review
- New roles for elongation factors in RNA polymerase II ubiquitylation and degradation.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023Review
- Methods to investigate nucleosome structure and dynamics with single-molecule FRET.Methods (San Diego, Calif.) · 2023Article
- Review
- Effects of Histone H2B Ubiquitylations and H3K79meACS chemical biology · 2023Article
- Structural basis of RNA polymerase II transcription on the chromatosome containing linker histone H1.Nature communications · 2022Article
- Uncovering the mechanisms of transcription elongation by eukaryotic RNA polymerases I, II, and III.iScience · 2022Article
- The pausing zone and control of RNA polymerase II elongation by Spt5: Implications for the pause-release model.Molecular cell · 2022Article
- Structural basis of nucleosome retention during transcription elongation.Science (New York, N.Y.) · 2022Article
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4 authors at 1 institution in 1 country.
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Abstract
RNA polymerase II (RNAPII) passes through the nucleosome in a coordinated manner, generating several intermediate nucleosomal states as it breaks and then reforms histone-DNA contacts ahead of and behind it, respectively. Several studies have defined transcription-induced nucleosome intermediates using only RNA Polymerase. However, RNAPII is decorated with elongation factors as it transcribes the genome. One such factor, Spt4/5, becomes an integral component of the elongation complex, making direct contact with the 'jaws' of RNAPII and nucleic acids in the transcription scaffold. We have characterized the effect of incorporating Spt4/5 into the elongation complex on transcription through the 601R nucleosome. Spt4/5 suppressed RNAPII pausing at the major H3/H4-induced arrest point, resulting in downstream re-positioning of RNAPII further into the nucleosome. Using a novel single molecule FRET system, we found that Spt4/5 affected the kinetics of DNA re-wrapping and stabilized a nucleosomal intermediate with partially unwrapped DNA behind RNAPII. Comparison of nucleosomes of different sequence polarities suggest that the strength of the DNA-histone interactions behind RNAPII specifies the Spt4/5 requirement. We propose that Spt4/5 may be important to coordinate the mechanical movement of RNAPII through the nucleosome with co-transcriptional chromatin modifications during transcription, which is affected by the strength of histone-DNA interactions.
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