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The histone chaperone sNASP binds a conserved peptide motif within the globular core of histone H3 through its TPR repeats
Eukaryotic chromatin is a complex yet dynamic structure, which is regulated in part by the assembly and disassembly of nucleosomes. Key to this process is a group of proteins termed histone chaperones that guide the thermodynamic assembly of nucleosomes by interacting with soluble histones. Here we...
Autores principales: | Bowman, Andrew, Lercher, Lukas, Singh, Hari R., Zinne, Daria, Timinszky, Gyula, Carlomagno, Teresa, Ladurner, Andreas G. |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2016
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4838342/ https://www.ncbi.nlm.nih.gov/pubmed/26673727 http://dx.doi.org/10.1093/nar/gkv1372 |
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