The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution

Bowman, Andrew; Hammond, Colin M.; Stirling, Andrew; Ward, Roger; Shang, Weifeng; Mkami, Hassane El; Robinson, David A.; Svergun, Dmitri I.; Norman, D.; Owen-Hughes, Tom

doi:10.1093/nar/gku232

Cited by 37 publications

(60 citation statements)

References 44 publications

(85 reference statements)

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“…The reported cellular functions of Vps75 and Nap1 are with H3–H4 and H2A–H2B, respectively, although both chaperones are capable of binding both H2A–H2B and H3–H4 in vitro 54,55 . Vps75 and, to a lesser extent, Nap1 are capable of forming tetrameric ring-like assemblies 51,56 and they further oligomerize upon histone binding 51,52,57 . Tetramerization of Vps75 (FIG.…”

Section: Mechanistic Insights Into Chaperoning Histonesmentioning

confidence: 99%

Histone chaperone networks shaping chromatin function

Hammond

Strømme

Huang

et al. 2017

Nat Rev Mol Cell Biol

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416

419

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The association of histones with specific chaperone complexes is important for their folding, oligomerization, post-translational modification, nuclear import, stability, assembly and genomic localization. In this way, the chaperoning of soluble histones is a key determinant of histone availability and fate, which affects all chromosomal processes, including gene expression, chromosome segregation and genome replication and repair. Here, we review the distinct structural and functional properties of the expanding network of histone chaperones. We emphasize how chaperones cooperate in the histone chaperone network and via co-chaperone complexes to match histone supply with demand, thereby promoting proper nucleosome assembly and maintaining epigenetic information by recycling modified histones evicted from chromatin.

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Section: Mechanistic Insights Into Chaperoning Histonesmentioning

confidence: 99%

Histone chaperone networks shaping chromatin function

Hammond

Strømme

Huang

et al. 2017

Nat Rev Mol Cell Biol

Self Cite

416

419

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“…The tetramer structure of histone chaperones in solution was modelled from an XRD-based dimer structure and DEER restraints, whereas SAXS curve fitting was used for testing for the correct global shape [64]. A similar approach was applied to a chromatin-remodelling enzyme [65].…”

Section: Integrative Modellingmentioning

confidence: 99%

The contribution of modern EPR to structural biology

Jeschke

2018

Emerging Topics in Life Sciences

133

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Electron paramagnetic resonance (EPR) spectroscopy combined with site-directed spin labelling is applicable to biomolecules and their complexes irrespective of system size and in a broad range of environments. Neither short-range nor long-range order is required to obtain structural restraints on accessibility of sites to water or oxygen, on secondary structure, and on distances between sites. Many of the experiments characterize a static ensemble obtained by shock-freezing. Compared with characterizing the dynamic ensemble at ambient temperature, analysis is simplified and information loss due to overlapping timescales of measurement and system dynamics is avoided. The necessity for labelling leads to sparse restraint sets that require integration with data from other methodologies for building models. The double electron-electron resonance experiment provides distance distributions in the nanometre range that carry information not only on the mean conformation but also on the width of the native ensemble. The distribution widths are often inconsistent with Anfinsen's concept that a sequence encodes a single native conformation defined at atomic resolution under physiological conditions.

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“…Pulsed methods such as pulsed electron–electron double resonance (PELDOR or DEER for double electron–electron resonance)2 and double quantum coherence3 (DQC)‐based experiments have shown potential for measuring distances up to 10 nm and beyond 4. These long‐range restraints are very informative for assigning a protein's conformational state.…”

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confidence: 99%

Accurate Extraction of Nanometer Distances in Multimers by Pulse EPR

Valera

Ackermann

Pliotas

et al. 2016

Chemistry A European J

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Pulse electron paramagnetic resonance (EPR) is gaining increasing importance in structural biology. The PELDOR (pulsed electron–electron double resonance) method allows extracting distance information on the nanometer scale. Here, we demonstrate the efficient extraction of distances from multimeric systems such as membrane‐embedded ion channels where data analysis is commonly hindered by multi‐spin effects.

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The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution

Cited by 37 publications

References 44 publications

Histone chaperone networks shaping chromatin function

Histone chaperone networks shaping chromatin function

The contribution of modern EPR to structural biology

Accurate Extraction of Nanometer Distances in Multimers by Pulse EPR

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