ArticleMethods (San Diego, Calif.)2019
Single-molecule FRET method to investigate the dynamics of transcription elongation through the nucleosome by RNA polymerase II.
Article in Methods (San Diego, Calif.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 24 citations in OpenAlex.
- Conformations of Linker Histone H1 Bound to Nucleosome Arrays.Journal of molecular biology · 2026Article
- Roles of histone chaperone Nap1 and histone acetylation in regulating phase-separation of nucleosome arrays.Nature communications · 2025Article
- Structural Characterization of Protein-Nucleic Acid Complexes: An Overview of the Recent Innovation in the Analytic Methods.International journal of molecular sciences · 2025Review
- Disentangling Timescales of Molecular Kinetics with spFRET using ALEX-FCS.Journal of fluorescence · 2025Article
- Histone H3 Tail Modifications Alter Structure and Dynamics of the H1 C-Terminal Domain Within Nucleosomes.Journal of molecular biology · 2023Article
- Methods to investigate nucleosome structure and dynamics with single-molecule FRET.Methods (San Diego, Calif.) · 2023Article
- Effects of Histone H2B Ubiquitylations and H3K79meACS chemical biology · 2023Article
- Recent Development in Biomedical Applications of Oligonucleotides with Triplex-Forming Ability.Polymers · 2023Review
- The Effects of Histone H2B Ubiquitylations on the Nucleosome Structure and Internucleosomal Interactions.Biochemistry · 2022Article
- DOT1L activity in leukemia cells requires interaction with ubiquitylated H2B that promotes productive nucleosome binding.Cell reports · 2022Article
- Conformational Dynamics of Poly(T) Single-Stranded DNA at the Single-Molecule Level.The journal of physical chemistry letters · 2021Article
- Single-Molecule Techniques to Study Chromatin.Frontiers in cell and developmental biology · 2021Review
- Nucleosome Dynamics during Transcription Elongation.ACS chemical biology · 2020Article
- PCNA Monoubiquitination Is Regulated by Diffusion of Rad6/Rad18 Complexes along RPA Filaments.Biochemistry · 2020Article
- Physical Chemistry of Epigenetics: Single-Molecule Investigations.The journal of physical chemistry. B · 2019Review
- Single-molecule FRET method to investigate the dynamics of transcription elongation through the nucleosome by RNA polymerase II.Methods (San Diego, Calif.) · 2019Article
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4 authors at 1 institution in 1 country.
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Abstract
Transcription elongation through the nucleosome is a precisely coordinated activity to ensure timely production of RNA and accurate regulation of co-transcriptional histone modifications. Nucleosomes actively participate in transcription regulation at various levels and impose physical barriers to RNA polymerase II (RNAPII) during transcription elongation. Despite its high significance, the detailed dynamics of how RNAPII translocates along nucleosomal DNA during transcription elongation and how the nucleosome structure dynamically conforms to the changes necessary for RNAPII progression remain poorly understood. Transcription elongation through the nucleosome is a complex process and investigating the changes of the nucleosome structure during this process by ensemble measurements is daunting. This is because it is nearly impossible to synchronize elongation complexes within a nucleosome or a sub-nucleosome to a designated location at a high enough efficiency for desired sample homogeneity. Here we review our recently developed single-molecule FRET experimental system and method that has fulfilled this deficiency. With our method, one can follow the changes in the structure of individual nucleosomes during transcription elongation. We demonstrated that this method enables the detailed measurements of the kinetics of transcription elongation through the nucleosome and its regulation by a transcription factor, which can be easily extended to investigations of the roles of environmental variables and histone post-translational modifications in regulating transcription elongation.
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