Conformational Dynamics of Histone H3 Tails in Chromatin
| Autor: | Matthew D. Shannon, Nicole Gonzalez Salguero, Christopher P. Jaroniec, Theint Theint, Mohamad Zandian, Michael G. Poirier, Rudra N. Purusottam |
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| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular Magnetic Resonance Spectroscopy Protein Conformation Static Electricity Supramolecular chemistry 010402 general chemistry 01 natural sciences Genome Article law.invention Histones 03 medical and health sciences Histone H3 chemistry.chemical_compound law Nucleosome General Materials Science Physical and Theoretical Chemistry 030304 developmental biology 0303 health sciences Chemistry DNA Linker DNA Chromatin 0104 chemical sciences Biophysics Recombinant DNA |
| Zdroj: | J Phys Chem Lett |
| ISSN: | 1948-7185 |
| Popis: | Chromatin is a supramolecular DNA-protein complex that compacts eukaryotic genomes and regulates their accessibility and functions. Dynamically disordered histone H3 N-terminal tails are among key chromatin regulatory components. Here, we used high-resolution-magic-angle-spinning NMR measurements of backbone amide (15)N spin relaxation rates to investigate, with residue-specific detail, the dynamics and interactions of H3 tails in recombinant (13)C,(15)N-enriched nucleosome arrays containing 15, 30 or 60 bp linker DNA between the nucleosome repeats. These measurements were compared to analogous data available for mononucleosomes devoid of linker DNA or containing two 20 bp DNA overhangs. The H3 tail dynamics in nucleosome arrays were found to be considerably attenuated compared to nucleosomes with or without linker DNA due to transient electrostatic interactions with the linker DNA segments and the structured chromatin environment. Remarkably, however, the H3 tail dynamics were not modulated by the specific linker DNA length within the 15–60 bp range investigated here. |
| Databáze: | OpenAIRE |
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