Toward an ensemble view of chromatosome structure: a paradigm shift from one to many
There is renewed interest in linker histone (LH)—nucleosome binding and how LHs influence eukaryotic DNA compaction. For a long time, the goal was to uncover “the structure of the chromatosome,” but recent studies of LH-nucleosome complexes have revealed an ensemble of structures. Notably, the recon...
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| Main Authors: | , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
August 7, 2018
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| In: |
Structure
Year: 2018, Volume: 26, Issue: 8, Pages: 1050-1057 |
| ISSN: | 1878-4186 |
| DOI: | 10.1016/j.str.2018.05.009 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.str.2018.05.009 Verlag, lizenzpflichtig, Volltext: http://www.sciencedirect.com/science/article/pii/S0969212618301734 
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| Author Notes: | Mehmet Ali Öztürk, Vlad Cojocaru, and Rebecca C. Wade |
| Summary: | There is renewed interest in linker histone (LH)—nucleosome binding and how LHs influence eukaryotic DNA compaction. For a long time, the goal was to uncover “the structure of the chromatosome,” but recent studies of LH-nucleosome complexes have revealed an ensemble of structures. Notably, the reconstituted LH-nucleosome complexes used in experiments rarely correspond to the sequence combinations present in organisms. For a full understanding of the determinants of the distribution of the chromatosome structural ensemble, studies must include a complete description of the sequences and experimental conditions used, and be designed to enable systematic evaluation of sequence and environmental effects. |
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| Item Description: | Gesehen am 10.03.2020 |
| Physical Description: | Online Resource |
| ISSN: | 1878-4186 |
| DOI: | 10.1016/j.str.2018.05.009 |