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Integrated Molecular Mechanism Directing Nucleosome Reorganization by Human FACT

Overview
Journal Genes Dev
Specialty Molecular Biology
Date 2016 Mar 12
PMID 26966247
Citations 85
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Abstract

Facilitates chromatin transcription (FACT) plays essential roles in chromatin remodeling during DNA transcription, replication, and repair. Our structural and biochemical studies of human FACT-histone interactions present precise views of nucleosome reorganization, conducted by the FACT-SPT16 (suppressor of Ty 16) Mid domain and its adjacent acidic AID segment. AID accesses the H2B N-terminal basic region exposed by partial unwrapping of the nucleosomal DNA, thereby triggering the invasion of FACT into the nucleosome. The crystal structure of the Mid domain complexed with an H3-H4 tetramer exhibits two separate contact sites; the Mid domain forms a novel intermolecular β structure with H4. At the other site, the Mid-H2A steric collision on the H2A-docking surface of the H3-H4 tetramer within the nucleosome induces H2A-H2B displacement. This integrated mechanism results in disrupting the H3 αN helix, which is essential for retaining the nucleosomal DNA ends, and hence facilitates DNA stripping from histone.

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References
1.
Sivolob A, Lavelle C, Prunell A . Sequence-dependent nucleosome structural and dynamic polymorphism. Potential involvement of histone H2B N-terminal tail proximal domain. J Mol Biol. 2003; 326(1):49-63. DOI: 10.1016/s0022-2836(02)01372-4. View

2.
Woodcock C, Ghosh R . Chromatin higher-order structure and dynamics. Cold Spring Harb Perspect Biol. 2010; 2(5):a000596. PMC: 2857170. DOI: 10.1101/cshperspect.a000596. View

3.
Pettersen E, Goddard T, Huang C, Couch G, Greenblatt D, Meng E . UCSF Chimera--a visualization system for exploratory research and analysis. J Comput Chem. 2004; 25(13):1605-12. DOI: 10.1002/jcc.20084. View

4.
Hondele M, Stuwe T, Hassler M, Halbach F, Bowman A, Zhang E . Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature. 2013; 499(7456):111-4. DOI: 10.1038/nature12242. View

5.
Otwinowski Z, Minor W . Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997; 276:307-26. DOI: 10.1016/S0076-6879(97)76066-X. View