Recognition of unmethylated histone H3 lysine 4 links BHC80 to LSD1-mediated gene repression

Fei Lan, Robert E. Collins, Rossella De Cegli, Roman Alpatov, John R. Horton, Xiaobing Shi, Or Gozani, Xiaodong Cheng () and Yang Shi ()
Additional contact information
Fei Lan: Harvard Medical School, 77 Ave Louis Pasteur, Boston, Massachusetts 02115, USA
Robert E. Collins: Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA
Rossella De Cegli: Harvard Medical School, 77 Ave Louis Pasteur, Boston, Massachusetts 02115, USA
Roman Alpatov: Harvard Medical School, 77 Ave Louis Pasteur, Boston, Massachusetts 02115, USA
John R. Horton: Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA
Xiaobing Shi: Stanford University, Stanford, California 94305, USA
Or Gozani: Stanford University, Stanford, California 94305, USA
Xiaodong Cheng: Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA
Yang Shi: Harvard Medical School, 77 Ave Louis Pasteur, Boston, Massachusetts 02115, USA

Nature, 2007, vol. 448, issue 7154, 718-722

Abstract: BHC80 is a component of the LSD1 co-repressor complex that demethylates histone H3 at lysine 4. The PHD domain of BHC80 interacts with the histone H3 tail only when lysine 4 is unmethylated, and BHC80 function is coupled to that of LSD1 in gene repression.

Date: 2007
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DOI: 10.1038/nature06034

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