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Nucleus. 2013 Nov-Dec;4(6):443-9. doi: 10.4161/nucl.27235. Epub 2013 Dec 5.

Catch me if you can: how the histone chaperone FACT capitalizes on nucleosome breathing.

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Department of Physiological Chemistry; Butenandt Institute and LMU Biomedical Center, Faculty of Medicine; Ludwig Maximilians University of Munich; Munich, Germany; Munich Cluster for Systems Neurology (SyNergy); Munich, Germany; Center for Integrated Protein Science Munich (CIPSM); Munich, Germany.


Nucleosomes confer a barrier to processes that require access to the eukaryotic genome such as transcription, DNA replication and repair. A variety of ATP-dependent nucleosome remodeling machines and ATP-independent histone chaperones facilitate nucleosome dynamics by depositing or evicting histones and unwrapping the DNA. It is clear that remodeling machines can use the energy from ATP to actively destabilize, translocate or disassemble nucleosomes. But how do ATP-independent histone chaperones, which "merely" bind histones, contribute to this process? Using our recent structural analysis of the conserved and essential eukaryotic histone chaperone FACT in complex with histones H2A-H2B as an example, we suggest that FACT capitalizes on transiently exposed surfaces of the nucleosome. By binding these surfaces, FACT stabilizes thermodynamically unfavorable intermediates of the intrinsically dynamic nucleosome particle. This makes the nucleosome permissive to DNA and RNA polymerases, providing temporary access, passage, and read-out.


chromatin; histone chaperone; nucleosome (reorganization); structure / crystallography; thermodynamics / kinetic of nucleosome (un)folding; transcription through chromatin

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