ArticleProceedings of the National Academy of Sciences of the United States of America2012
Regulation of the H4 tail binding and folding landscapes via Lys-16 acetylation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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51 citing papers in PubMed, 90 citations in OpenAlex.
- Energy Landscapes and Structural Plasticity of Intrinsically Disordered Histones.Journal of chemical information and modeling · 2025Article
- Unveiling the Conformational Dynamics of the Histone Tails Using Markov State Modeling.Journal of chemical theory and computation · 2025Article
- Connected Chromatin Amplifies Acetylation-Modulated Nucleosome Interactions.Biochemistry · 2025Article
- Conformational Dynamics of the Nucleosomal Histone H2B Tails Revealed by Molecular Dynamics Simulations.Journal of chemical information and modeling · 2024Article
- Beyond the tail: the consequence of context in histone post-translational modification and chromatin research.The Biochemical journal · 2024Article
- The role of cryptic ancestral symmetry in histone folding mechanisms across Eukarya and Archaea.PLoS computational biology · 2024Article
- Multiscale Modeling of Protein-RNA Condensation in and Out of Equilibrium.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Chromatin fiber breaks into clutches under tension and crowding.Nucleic acids research · 2022Article
- Phase Separation and Correlated Motions in Motorized Genome.The journal of physical chemistry. B · 2022Article
- Quantifying epigenetic modulation of nucleosome breathing by high-throughput AFM imaging.Biophysical journal · 2022Article
- RNA length has a non-trivial effect in the stability of biomolecular condensates formed by RNA-binding proteins.PLoS computational biology · 2022Article
- The regional sequestration of heterochromatin structural proteins is critical to form and maintain silent chromatin.Epigenetics & chromatin · 2022Review
- Post-translational insertion of boron in proteins to probe and modulate function.Nature chemical biology · 2021Article
- Histone Tail Conformations: A Fuzzy Affair with DNA.Trends in biochemical sciences · 2021Review
- Solvent Exposure and Ionic Condensation Drive Fuzzy Dimerization of Disordered Heterochromatin Protein Sequence.Biomolecules · 2021Article
- Binding Dynamics of Disordered Linker Histone H1 with a Nucleosomal Particle.Journal of molecular biology · 2021Article
- Stability and folding pathways of tetra-nucleosome from six-dimensional free energy surface.Nature communications · 2021Article
- High resolution ensemble description of metamorphic and intrinsically disordered proteins using an efficient hybrid parallel tempering scheme.Nature communications · 2021Article
- Expansion of Intrinsically Disordered Proteins Increases the Range of Stability of Liquid-Liquid Phase Separation.Molecules (Basel, Switzerland) · 2020Article
- Protein disorder-to-order transition enhances the nucleosome-binding affinity of H1.Nucleic acids research · 2020Article
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2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intrinsically disordered proteins (IDP) are a broad class of proteins with relatively flat energy landscapes showing a high level of functional promiscuity, which are frequently regulated through posttranslational covalent modifications. Histone tails, which are the terminal segments of the histone proteins, are prominent IDPs that are implicated in a variety of signaling processes, which control chromatin organization and dynamics. Although a large body of work has been done on elucidating the roles of posttranslational modifications in functional regulation of IDPs, molecular mechanisms behind the observed behaviors are not fully understood. Using extensive atomistic molecular dynamics simulations, we found in this work that H4 tail mono-acetylation at LYS-16, which is a key covalent modification, induces a significant reorganization of the tail's conformational landscape, inducing partial ordering and enhancing the propensity for alpha-helical segments. Furthermore, our calculations of the potentials of mean force between the H4 tail and a DNA fragment indicate that contrary to the expectations based on simple electrostatic reasoning, the Lys-16 mono-acetylated H4 tail binds to DNA stronger than the unacetylated protein. Based on these results, we propose a molecular mechanism for the way Lys-16 acetylation might lead to experimentally observed disruption of compact chromatin fibers.
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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.