The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution
NAP-1 fold histone chaperones play an important role in escorting histones to and from sites of nucleosome assembly and disassembly. The two NAP-1 fold histone chaperones in budding yeast, Vps75 and Nap1, have previously been crystalized in a characteristic homodimeric conformation. In this study, a...
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| Veröffentlicht in: | Nucleic acids research 2014-05, Vol.42 (9), p.6038-6051 |
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| container_title | Nucleic acids research |
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| creator | Bowman, Andrew Hammond, Colin M. Stirling, Andrew Ward, Richard Shang, Weifeng El-Mkami, Hassane Robinson, David A. Svergun, Dmitri I. Norman, David G. Owen-Hughes, Tom |
| description | NAP-1 fold histone chaperones play an important role in escorting histones to and from sites of nucleosome assembly and disassembly. The two NAP-1 fold histone chaperones in budding yeast, Vps75 and Nap1, have previously been crystalized in a characteristic homodimeric conformation. In this study, a combination of small angle X-ray scattering, multi angle light scattering and pulsed electron–electron double resonance approaches were used to show that both Vps75 and Nap1 adopt ring-shaped tetrameric conformations in solution. This suggests that the formation of homotetramers is a common feature of NAP-1 fold histone chaperones. The tetramerisation of NAP-1 fold histone chaperones may act to shield acidic surfaces in the absence of histone cargo thus providing a ‘self-chaperoning’ type mechanism. |
| doi_str_mv | 10.1093/nar/gku232 |
| format | Article |
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The tetramerisation of NAP-1 fold histone chaperones may act to shield acidic surfaces in the absence of histone cargo thus providing a ‘self-chaperoning’ type mechanism.</description><identifier>ISSN: 0305-1048</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/gku232</identifier><identifier>PMID: 24688059</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Models, Molecular ; Molecular Chaperones - chemistry ; Nucleosome Assembly Protein 1 - chemistry ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Structure, Quaternary ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins - chemistry ; Scattering, Small Angle ; Solutions ; Structural Biology ; X-Ray Diffraction</subject><ispartof>Nucleic acids research, 2014-05, Vol.42 (9), p.6038-6051</ispartof><rights>The Author(s) 2014. 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| subjects | Models, Molecular Molecular Chaperones - chemistry Nucleosome Assembly Protein 1 - chemistry Protein Binding Protein Interaction Domains and Motifs Protein Structure, Quaternary Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins - chemistry Scattering, Small Angle Solutions Structural Biology X-Ray Diffraction |
| title | The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution |
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