Bromo adjacent homology domain containing 1(BAHD1) is a protein that in humans is encoded by the BAHD1 gene. BAHD1 is involved in heterochromatin formation and transcriptional repression. [5]
Bromo adjacent homology domain containing 1(BAHD1) is a protein that in humans is encoded by the BAHD1 gene. BAHD1 is involved in heterochromatin formation and transcriptional repression. [5]
BAHD1 was first cloned from a human brain cDNA library and the coding sequence was named KIAA0945. [6] Bierne and colleagues further discovered the function of BAHD1 in the regulation of chromatin structure and gene expression. [7]
BAHD1 acts as a co-repressor by interacting with a set of proteins that promote chromatin compaction and regulate transcription. [7] [8] Tandem-affinity purification of the BAHD1-associated protein complex in human HEK293 cells identified MIER proteins (MIER1, MIER2, MIER3), histone deacetylase HDAC1 and HDAC2, histone H3K9 methyltransferase EHMT2, heterochromatin protein 1 (HP1 alpha, HP1 beta, HP1 gamma), MBD1, TRIM28 and CDYL as partners of BAHD1. [8] Overexpression of BAHD1 in HEK293 cells induces large-scale chromatin condensation [7] and DNA methylation on autosomes. [9] The C-terminal BAH domain of BAHD1 acts as a reader for the epigenetic mark H3K27me3. [10] Ectopically expressed BAHD1 colocalizes with the heterochromatic inactive X chromosome (Xi). [7] [9]
Ablation of the Bahd1 gene in the mouse alters placental development and results in hypocholesterolemia, hypoglycemia and decreased body fat. [8] Bahd1-haplodeficiency in mice decreases the efficiency of infection with the bacterial pathogen Listeria monocytogenes . [11]
During infection of human epithelial cells with the pathogen Listeria monocytogenes , BAHD1 represses interferon-stimulated genes. [11] At specific stages of infection, a Listeria nucleomodulin, LntA, acts as an inhibitor of BAHD1 and activates interferon-stimulated genes. [11] [12] The BAHD1 gene is downregulated in the colon tissue in a mouse model of ulcerative colitis. [13]
Listeriolysin O (LLO) is a hemolysin produced by the bacterium Listeria monocytogenes, the pathogen responsible for causing listeriosis. The toxin may be considered a virulence factor, since it is crucial for the virulence of L. monocytogenes.
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