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...

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Detalles Bibliográficos
Autores principales: Bowman, Andrew, Lercher, Lukas, Singh, Hari R., Zinne, Daria, Timinszky, Gyula, Carlomagno, Teresa, Ladurner, Andreas G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2016
Materias:
Gene regulation, Chromatin and Epigenetics
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

Internet

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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