Disease relevance of BRD7

• In addition, the expression levels of NAG-7, and BRD7 did not alter in gastric and colorectal cancers [1].

High impact information on BRD7

• Moreover, we observed that BRD7 could regulate the promoter activity of E2F3, one of its targets [2].
• In the present study, tet-on inducible expression system was used to investigate the role of BRD7 in cell growth and cell cycle progression [2].
• BRD7 is a novel bromodomain gene and it is downexpressed in nasopharyngeal carcinoma (NPC) biopsies and cell lines; its function is poorly understood [2].
• Disruption of the E1B-AP5-BRD7 complex increased E1B-AP5 repression activity for basic transcription and converted it from being an activator of the hormone-dependent promoter into being a strong repressor [3].
• Using yeast two-hybrid screening, we identified a novel chromatin-associated bromodomain-containing protein, BRD7, as an E1B-AP5 interaction partner [3].

Biological context of BRD7

• To identify proteins that interact with cell-cycle regulatory factors, we performed yeast two-hybrid analysis with IRF-2 and identified a novel human protein termed Celtix-1 which binds to IRF-2 [4].
• In addition, no obvious changes were observed in the acetylated level of histone H3 after transfection with BRD7, indicating that chromatin remodeling, not chromatin modification, is the major mechanism of BRD7 mediated gene transcription [5].
• Little is known about the transcriptional mechanisms controlling BRD7 gene expression [6].
• In this paper, we have characterized the 5' regulatory region of the BRD7 gene in order to understand the molecular mechanisms regulating its expression [6].
• Taken together, these results will help to better understand the role of the BRD7 gene in signal-dependent transcriptional regulation, and to develop new reagents for therapeutic upregulation of the BRD7 gene in NPC [6].

Physical interactions of BRD7

• More importantly, wild-type BRD7 interacted with H3 peptide acetylated at Lys14, while the bromodomain deleted mutant lost this ability [5].

Other interactions of BRD7

• We conclude that the bromodomain protein Celtix-1 is a novel IRF-2 interacting protein that associates with transcriptionally active chromatin in situ [4].
• This seems to suggest that NAG-7 and BRD7 genes may not play a role in gastric and colorectal carcinogenesis [1].
• Expression of tumor related genes NGX6, NAG-7, BRD7 in gastric and colorectal cancer [1].
• We confirmed E1B-AP5-BRD7 complex formation in vivo and in vitro [3].
• In the present study, we revealed the co-localization between acetylated H3 and BRD7 and found that the bromodomain of BRD7 is required for this co-localization [5].

Analytical, diagnostic and therapeutic context of BRD7

• Using a panel of IRF-2 deletion mutants in yeast two-hybrid assays, we established that Celtix-1 contacts the C-terminus of IRF-2 [4].
• We further performed cell cycle cDNA array to screen potential transcriptional targets of BRD7 in cell cycle [2].
• RESULTS: Homology-based sequence analysis revealed that the bromodomain of BRD-7 possibly contains four alpha helices (Z, A, B and C), and a hydrophobic pocket which is an important structure to recognize acetylated histone peptide [7].

References