Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b

Lei Zeng, Qiang Zhang, SiDe Li, Alexander N. Plotnikov, Martin J. Walsh and Ming-Ming Zhou ()
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Lei Zeng: Mount Sinai School of Medicine, 1425 Madison Avenue, Box 1677, New York, New York 10029, USA
Qiang Zhang: Mount Sinai School of Medicine, 1425 Madison Avenue, Box 1677, New York, New York 10029, USA
SiDe Li: Mount Sinai School of Medicine
Alexander N. Plotnikov: Mount Sinai School of Medicine, 1425 Madison Avenue, Box 1677, New York, New York 10029, USA
Martin J. Walsh: Mount Sinai School of Medicine, 1425 Madison Avenue, Box 1677, New York, New York 10029, USA
Ming-Ming Zhou: Mount Sinai School of Medicine, 1425 Madison Avenue, Box 1677, New York, New York 10029, USA

Nature, 2010, vol. 466, issue 7303, 258-262

Abstract: Reading histone acetylation Histone lysine acetylation or methylation helps to regulate chromatin functions during gene transcription. Histone acetylation marks are typically recognized by proteins containing bromodomains, but recently, an alternative mechanism of acetyl-lysine binding was recognized in the tandem plant homeodomain (PHD) finger of human DPF3b, a protein that functions in gene activation. The three-dimensional solution structures of DPF3b bound to a lysine 14-acetylated histone H3 peptide have now been determined, offering mechanistic insight into the way the protein recognizes acetylation marks.

Date: 2010
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DOI: 10.1038/nature09139

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