Regulation of Nucleosome Stacking and Chromatin Compaction by the Histone H4 N-Terminal Tail–H2A Acidic Patch Interaction

Chen, Qinming; Yang, Renliang; Korolev, Nikolay; Liu, Chuan Fa; Nordenskiöld, Lars

doi:10.1016/j.jmb.2017.03.016

Cited by 61 publications

(46 citation statements)

References 63 publications

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“…These results confirm a two-start fiber organization with a type II interface on both sides of each nucleosome, strongly validating our 6-mer crystal structure. We note that the type II interface is also compatible with three additional H4-H2A and H4-H2B internucleosome crosslinks recently reported for a 12-nucleosome array in solution (Chen et al, 2017;Figures S4B and S4C).…”

Section: Crosslinking Confirms a Two-start Structure With Uniform Intsupporting

confidence: 89%

Structure of an H1-Bound 6-Nucleosome Array Reveals an Untwisted Two-Start Chromatin Fiber Conformation

et al. 2018

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Section: Crosslinking Confirms a Two-start Structure With Uniform Intsupporting

confidence: 89%

Structure of an H1-Bound 6-Nucleosome Array Reveals an Untwisted Two-Start Chromatin Fiber Conformation

et al. 2018

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“…In other NCP structures (27,36,(66)(67)(68)(69)(70), the basic H4 tail 16-23 aa domain mediates nucleosome stacking by interacting with the acidic patch of H2A-H2B located on the surface of the neighbouring HO core and thereby regulates chromatin fibre compaction (27,36,(66)(67)(68)(69)(70). We wondered whether this H4 tail interaction was also present in the Telo-NCP crystal structure, which would suggest a similar stabilisation of telomeric chromatin compaction by H4 tail-mediated nucleosome-nucleosome stacking.…”

Section: The Basic H4 N-terminal Tail Interacts With the Ho Acidic Pamentioning

confidence: 96%

The human telomeric nucleosome displays distinct structural and dynamic properties

Soman

Liew

Teo

et al. 2019

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ABSTRACTTelomeres protect the ends of our chromosomes and are key to maintaining genomic integrity during cell division and differentiation. However, our knowledge of telomeric chromatin and nucleosome structure at the molecular level is limited. Here, we aimed to define the structure, dynamics as well as properties in solution of the human telomeric nucleosome. We first determined the 2.2 Å crystal structure of a human telomeric nucleosome core particle (NCP) containing 145 bp DNA, which revealed the same helical path for the DNA as well as symmetric stretching in both halves of the NCP as that of the 145 bp ‘601’ NCP. In solution, the telomeric nucleosome exhibited a less stable and a markedly more dynamic structure compared to NCPs containing DNA positioning sequences. These observations provide molecular insights into how telomeric DNA forms nucleosomes and chromatin and advance our understanding of the unique biological role of telomeres.

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“…In the genome, nucleosomes are spaced by so-called linker DNA of 20-90 bps 13,14 , but they can nonetheless interact with each other via histone tails to form higher-order chromatin structures, e.g., fibers 15,16 . The topology of such chromatin fibers in vivo has remained a matter of debate, in part due to the heterogeneity of chromatin and its dynamic nature [17][18][19] .…”

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confidence: 99%

“…However, as the use of a low salt buffer in these experiments prevented the folding of nucleosomal arrays into compact fibers, neither the stacking between nucleosomes nor DNA unwrapping from nucleosomes could be probed. Under conditions that more closely resemble the in vivo context (i.e., 100 mM KCl and 2 mM MgCl 2 ), nucleosomes are known to stack into a condensed fiber 16 , and the torsional response is therefore expected to differ.…”

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confidence: 99%

Chromatin fibers stabilize nucleosomes under torsional stress

et al. 2020

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Torsional stress generated during DNA replication and transcription has been suggested to facilitate nucleosome unwrapping and thereby the progression of polymerases. However, the propagation of twist in condensed chromatin remains yet unresolved. Here, we measure how force and torque impact chromatin fibers with a nucleosome repeat length of 167 and 197. We find that both types of fibers fold into a left-handed superhelix that can be stabilized by positive torsion. We observe that the structural changes induced by twist were reversible, indicating that chromatin has a large degree of elasticity. Our direct measurements of torque confirmed the hypothesis of chromatin fibers as a twist buffer. Using a statistical mechanicsbased torsional spring model, we extracted values of the chromatin twist modulus and the linking number per stacked nucleosome that were in good agreement with values measured here experimentally. Overall, our findings indicate that the supercoiling generated by DNAprocessing enzymes, predicted by the twin-supercoiled domain model, can be largely accommodated by the higher-order structure of chromatin.

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Regulation of Nucleosome Stacking and Chromatin Compaction by the Histone H4 N-Terminal Tail–H2A Acidic Patch Interaction

Cited by 61 publications

References 63 publications

Structure of an H1-Bound 6-Nucleosome Array Reveals an Untwisted Two-Start Chromatin Fiber Conformation

Structure of an H1-Bound 6-Nucleosome Array Reveals an Untwisted Two-Start Chromatin Fiber Conformation

The human telomeric nucleosome displays distinct structural and dynamic properties

Chromatin fibers stabilize nucleosomes under torsional stress

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