Accessibility of the histone H3 tail in the nucleosome for binding of paired readers

Accessibility of the histone H3 tail in the nucleosome for binding of paired readers

The chromatin remodeller CHD4 contains two PHD finger reader domains that have been shown to bivalently recognize H3 histone tails. Here, the authors describe a mechanism by which the PHD fingers bind to the intact nucleosome core particle, revealing both cooperative and individual interactions.

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Bibliographic Details
Main Authors: Jovylyn Gatchalian, Xiaodong Wang, Jinzen Ikebe, Khan L. Cox, Adam H. Tencer, Yi Zhang, Nathaniel L. Burge, Luo Di, Matthew D. Gibson, Catherine A. Musselman, Michael G. Poirier, Hidetoshi Kono, Jeffrey J. Hayes, Tatiana G. Kutateladze
Format: article
Language:EN
Published: Nature Portfolio 2017
Subjects:
Science
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Online Access:https://doaj.org/article/80503b36d74a4bc3b72aa20bc28f7b84
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Summary:The chromatin remodeller CHD4 contains two PHD finger reader domains that have been shown to bivalently recognize H3 histone tails. Here, the authors describe a mechanism by which the PHD fingers bind to the intact nucleosome core particle, revealing both cooperative and individual interactions.

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