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

Maria Hondele, Tobias Stuwe, Markus Hassler, Felix Halbach, Andrew Bowman, Elisa T. Zhang, Bianca Nijmeijer, Christiane Kotthoff, Vladimir Rybin, Stefan Amlacher, Ed Hurt and Andreas G. Ladurner ()
Additional contact information
Maria Hondele: Butenandt Institute and LMU Biomedical Center, Faculty of Medicine, Ludwig Maximilians University of Munich, Butenandtstrasse 5, 81377 Munich, Germany
Tobias Stuwe: Genome Biology Unit and Structural & Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany
Markus Hassler: Butenandt Institute and LMU Biomedical Center, Faculty of Medicine, Ludwig Maximilians University of Munich, Butenandtstrasse 5, 81377 Munich, Germany
Felix Halbach: Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
Andrew Bowman: Butenandt Institute and LMU Biomedical Center, Faculty of Medicine, Ludwig Maximilians University of Munich, Butenandtstrasse 5, 81377 Munich, Germany
Elisa T. Zhang: Genome Biology Unit and Structural & Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany
Bianca Nijmeijer: Genome Biology Unit and Structural & Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany
Christiane Kotthoff: Butenandt Institute and LMU Biomedical Center, Faculty of Medicine, Ludwig Maximilians University of Munich, Butenandtstrasse 5, 81377 Munich, Germany
Vladimir Rybin: Genome Biology Unit and Structural & Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany
Stefan Amlacher: Biochemistry Center, University of Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany
Ed Hurt: Biochemistry Center, University of Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany
Andreas G. Ladurner: Butenandt Institute and LMU Biomedical Center, Faculty of Medicine, Ludwig Maximilians University of Munich, Butenandtstrasse 5, 81377 Munich, Germany

Nature, 2013, vol. 499, issue 7456, 111-114

Abstract: 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.

Date: 2013
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DOI: 10.1038/nature12242

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