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Structural basis of histone H2A-H2B recognition by the essential chaperone FACT

The crystal structure of the FACT histone chaperone domain Spt16M in complex with the H2A-H2B heterodimer is solved; Spt16M makes several interactions with histones and seems to block the interaction of H2B with DNA, which could explain how FACT destabilizes nucleosomes to promote transcription.

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Bibliographic Details
Main Authors: Hondele, Maria (Author) , Stuwe, Tobias (Author) , Hassler, Markus (Author) , Halbach, Felix (Author) , Bowman, Andrew (Author) , Zhang, Elisa T. (Author) , Nijmeijer, Bianca (Author) , Kotthoff, Christiane (Author) , Rybin, Vladimir (Author) , Amlacher, Stefan (Author) , Hurt, Ed (Author) , Ladurner, Andreas G. (Author)
Format: Article (Journal)
Language:English
Published: 22 May 2013
In: Nature
Year: 2013, Volume: 499, Issue: 7456, Pages: 111-114
ISSN:1476-4687
DOI:10.1038/nature12242
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/nature12242
Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/nature12242
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Author Notes:Maria Hondele, Tobias Stuwe, Markus Hassler, Felix Halbach, Andrew Bowman, Elisa T. Zhang, Bianca Nijmeijer, Christiane Kotthoff, Vladimir Rybin, Stefan Amlacher, Ed Hurt & Andreas G. Ladurner
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Summary:The crystal structure of the FACT histone chaperone domain Spt16M in complex with the H2A-H2B heterodimer is solved; Spt16M makes several interactions with histones and seems to block the interaction of H2B with DNA, which could explain how FACT destabilizes nucleosomes to promote transcription.
Item Description:Gesehen am 21.09.2021
Physical Description:Online Resource
ISSN:1476-4687
DOI:10.1038/nature12242

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