Fig. 1: The S phase-enriched BAHCC1 harbors a conserved tandem-Tudor domain (BAHCC1TTD) for specific readout of H4K20me1.
From: BAHCC1 binds H4K20me1 to facilitate the MCM complex loading and DNA replication
a Domain architecture of human BAHCC1 and mouse Bahcc1. TTD, tandem-Tudor domain; BAH, Bromo adjacent homology. b Time-course measurement for chromatin association of the indicated protein or histone modification in HeLa cells, released from a double thymidine block-induced early S arrest. Cell cycle phase and time post-release are indicated on the top. Experiment was repeated twice with similar results. c Alignment of BAHCC1TTD amino acid sequences from different species. Homo, Homo sapiens; Mus, Mus musculus; Bov, Bovine; Zeb, Zebrafish; Dme, Drosophila melanogaster. d Histone peptide arrays probed with the purified recombinant protein of GST-Bahcc1TTD, followed by α-GST immunoblot. Red boxes show the position of peptides with H4K20 methylation, with red color-highlighted peptides corresponding the strongest binding in each box. ac, acetylated; me1, mono-methylated; me2a, asymmetrically di-methylated; me2s, symmetrically di-methylated; me3, tri-methylated. e Pull-down for GST-53BP1TTD (top) or GST-Bahcc1TTD (middle) using biotinylated peptide with the indicated H4K20 methylation (lanes 1–4), followed by α-GST immunoblot. Bottom panel shows the peptide staining. f Isothermal Titration Calorimetry (ITC) assay measuring the affinity of Bahcc1TTD binding to histone peptide with the indicated H4K20 methylation. Kd, dissociation constant; n.m., not measurable. Source data are provided as a Source Data file.
