ArticleThe journal of physical chemistry. B2016
Single-Molecule Observation Reveals Spontaneous Protein Dynamics in the Nucleosome.
Article in The journal of physical chemistry. B, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Initiation of base excision repair is modulated by nucleosome occupancy modifying sequences.DNA repair · 2025Article
- Methods to investigate nucleosome structure and dynamics with single-molecule FRET.Methods (San Diego, Calif.) · 2023Article
- Ionic strength modulates excision of uracil by SMUG1 from nucleosome core particles.DNA repair · 2023Article
- Studying Chromatin Epigenetics with Fluorescence Microscopy.International journal of molecular sciences · 2022Review
- Nucleosome Dynamics during Transcription Elongation.ACS chemical biology · 2020Article
- Dynamics of the nucleosomal histone H3 N-terminal tail revealed by high precision single-molecule FRET.Nucleic acids research · 2020Article
- Physical Chemistry of Epigenetics: Single-Molecule Investigations.The journal of physical chemistry. B · 2019Review
- Global Repair Profile of Human Alkyladenine DNA Glycosylase on Nucleosomes Reveals DNA Packaging Effects.ACS chemical biology · 2019Article
- Molecular recognition of nucleosomes by binding partners.Current opinion in structural biology · 2019Review
- Single-molecule FRET method to investigate the dynamics of transcription elongation through the nucleosome by RNA polymerase II.Methods (San Diego, Calif.) · 2019Article
- How Protein Binding Sensitizes the Nucleosome to Histone H3K56 Acetylation.ACS chemical biology · 2019Article
- High precision FRET studies reveal reversible transitions in nucleosomes between microseconds and minutes.Nature communications · 2018Article
- Initiating base excision repair in chromatin.DNA repair · 2018Review
- Human OGG1 activity in nucleosomes is facilitated by transient unwrapping of DNA and is influenced by the local histone environment.DNA repair · 2017Article
- Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Structural dynamics of a protein molecule is often critical to its function. Single-molecule methods provide efficient ways to investigate protein dynamics, although it is very challenging to achieve a millisecond or higher temporal resolution. Here we report spontaneous structural dynamics of the histone protein core in the nucleosome based on a single-molecule method that can reveal submillisecond dynamics by combining maximum likelihood estimation and fluorescence correlation spectroscopy. The nucleosome, comprising ∼147 bp DNA and an octameric histone protein core consisting of H2A, H2B, H3, and H4, is the fundamental packing unit of the eukaryotic genome. The nucleosome imposes a physical barrier that should be overcome during various DNA-templated processes. Structural fluctuation of the nucleosome in the histone core has been hypothesized to be required for nucleosome disassembly but has yet to be directly probed. Our results indicate that at 100 mM NaCl the histone H2A-H2B dimer dissociates from the histone core transiently once every 3.6 ± 0.6 ms and returns to its position within 2.0 ± 0.3 ms. We also found that the motion is facilitated upon H3K56 acetylation and inhibited upon replacing H2A with H2A.Z. These results provide the first direct examples of how a localized post-translational modification or an epigenetic variation affects the kinetic and thermodynamic stabilities of a macromolecular protein complex, which may directly contribute to its functions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.