ArticleJournal of molecular biology2018
Site-Specific Disulfide Crosslinked Nucleosomes with Enhanced Stability.
Article in Journal of molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- DNA-histone cross-link locks the nucleosome structure and disrupts its recognition and processing.Protein & cell · 2026Article
- Stabilization of the hexasome intermediate during histone exchange by yeast SWR1 complex.Molecular cell · 2024Article
- Reorientation of INO80 on hexasomes reveals basis for mechanistic versatility.Science (New York, N.Y.) · 2023Article
- Expressed Protein Ligation without Intein.Journal of the American Chemical Society · 2020Article
- Molecular engineering strategies for visualizing low-affinity protein complexes.Experimental biology and medicine (Maywood, N.J.) · 2019Article
- Structures of the ISWI-nucleosome complex reveal a conserved mechanism of chromatin remodeling.Nature structural & molecular biology · 2019Article
- Article
- Bend-Induced Twist Waves and the Structure of Nucleosomal DNA.Physical review letters · 2018Article
- Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We engineered nucleosome core particles (NCPs) with two site-specific cysteine crosslinks that increase the stability of the particle. The first disulfide was introduced between the two copies of H2A via an H2A-N38C point mutation, effectively crosslinking the two H2A/H2B heterodimers together to stabilize the histone octamer against H2A/H2B dimer dissociation. The second crosslink was engineered between an R40C point mutation on the N-terminal tail of H3 and the NCP DNA ends by the introduction of a convertible nucleotide. This crosslink maintains the nucleosome DNA in a fixed translational setting relative to the histone octamer and prevents dilution-driven dissociation. The X-ray crystal structures of NCPs containing the disulfides in isolation and in combination were determined. Both disulfides stabilize the structure of the NCP without disturbing the overall structure. Nucleosomes containing these modifications will be advantageous for biochemical and structural studies as a consequence of their greater resistance to dissociation during high dilution in purification, elevated salt for crystallization and vitrification for cryogenic electron microscopy.
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Registered trials
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