An aromatic cage is required but not sufficient for binding of Tudor domains of the Polycomblike protein family to H3K36me3.
Jovylyn Gatchalian, Molly C Kingsley, Stacey D Moslet, Ruben D Rosas Ospina, Tatiana G Kutateladze
Author Information
Jovylyn Gatchalian: a Department of Pharmacology; University of Colorado School of Medicine ; Aurora , CO , USA.
Polycomblike (Pcl) proteins are important transcriptional regulators and components of the Polycomb Repressive Complex 2 (PRC2). The Tudor domains of human homologs PHF1 and PHF19 have been found to recognize trimethylated lysine 36 of histone H3 (H3K36me3); however, the biological role of Tudor domains of other Pcl proteins remains poorly understood. Here, we characterize the molecular basis underlying histone binding activities of the Tudor domains of the Pcl family. In contrast to a predominant view, we found that the methyl lysine-binding aromatic cage is necessary but not sufficient for recognition of H3K36me3 by these Tudor domains and that a hydrophobic patch, adjacent to the aromatic cage, is also required.
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F31 CA189487/NCI NIH HHS
R01 GM100907/NIGMS NIH HHS
R01 GM106416/NIGMS NIH HHS
GM100907/NIGMS NIH HHS
Binding Sites
DNA-Binding Proteins
Epigenesis, Genetic
Histone-Lysine N-Methyltransferase
Humans
Hydrophobic and Hydrophilic Interactions
Methylation
Nuclear Magnetic Resonance, Biomolecular
Polycomb Repressive Complex 2
Polycomb-Group Proteins
Protein Binding
Protein Conformation
Protein Structure, Tertiary
DNA-Binding Proteins
MTF2 protein, human
PHF1 protein, human
Polycomb-Group Proteins
Histone-Lysine N-Methyltransferase
Polycomb Repressive Complex 2
