摘要
Dear Editor,Histone recognition by reader modules constitutes a major mechanism for epigenetic regulation （Jenuwein and Allis 2001）. BAHD1 （bromo adjacent homology domain containing protein 1） is a vertebrate-specific nuclear protein （Fig. S1） involved in gene silencing by promoting heterochromatin formation. BAHD1 is characteristic with an N-terminal proline-rich region, a nuclear localization signal motif, and a C-terminal bromo adjacent homology （BAH） domain （Fig. 1A）. Previous study revealed that BAHD1 could act as a scaffold protein and tether diverse heterochromatinassociated factors including HP1, MBD1, SETDB1, HDAC5, and several transcriptional factors to trigger facultative heterochromatin formation （Bierne, Tham et al. 2009）. Consistent with a ＂repressive＂ role, BAHD1 binds to CpG-rich P3 promoter region of IGF2 （insulin-like growth factor II） then represses IGF2 and IGF2 antisense transcription via the recruitment of MBD1 and HDAC5 （Bierne, Tham et al. 2009）.
Dear Editor,Histone recognition by reader modules constitutes a major mechanism for epigenetic regulation （Jenuwein and Allis 2001）. BAHD1 （bromo adjacent homology domain containing protein 1） is a vertebrate-specific nuclear protein （Fig. S1） involved in gene silencing by promoting heterochromatin formation. BAHD1 is characteristic with an N-terminal proline-rich region, a nuclear localization signal motif, and a C-terminal bromo adjacent homology （BAH） domain （Fig. 1A）. Previous study revealed that BAHD1 could act as a scaffold protein and tether diverse heterochromatinassociated factors including HP1, MBD1, SETDB1, HDAC5, and several transcriptional factors to trigger facultative heterochromatin formation （Bierne, Tham et al. 2009）. Consistent with a ＂repressive＂ role, BAHD1 binds to CpG-rich P3 promoter region of IGF2 （insulin-like growth factor II） then represses IGF2 and IGF2 antisense transcription via the recruitment of MBD1 and HDAC5 （Bierne, Tham et al. 2009）.
