Disease relevance of BRF2

• BRFU has no specificity for sequences flanking the TATA-box and also forms a stable complex on the TATA-box of the pol II-specific adenovirus major late promoter (AdMLP) [1].
• Apolipoprotein B gene regulatory factor-2 (BRF-2) is structurally and immunologically highly related to hepatitis B virus X associated protein-1 (XAP-1) [2].

High impact information on BRF2

• In contrast, CK2 phosphorylation of TBP, Brf2, and Bdp1 combined is inhibitory [3].
• A stable complex of a novel transcription factor IIB- related factor, human TFIIIB50, and associated proteins mediate selective transcription by RNA polymerase III of genes with upstream promoter elements [4].
• We show that derivatives of mini-SNAP(c) lacking this region are active for transcription and that with such complexes, TBP can still be recruited to the U6 promoter through cooperative interactions with Brf2 [5].
• In addition, basal U6 transcription requires the SANT domain protein Bdp1 and the transcription factor IIB-related factor Brf2 [5].
• In addition, we have identified a GC-rich sequence downstream from the TATA box (the BURE) which, depending on the strength of TATA box, can either enhance BRFU binding to the TBP.DNA complex or hB" association with the BRFU.TBP.DNA complex, and subsequently stimulate pol III transcription [6].

Biological context of BRF2

• The genes FLJ14299, C8orf2, BRF2 and RAB11FIP, map within the 8p11-12 minimal amplicon, two have a putative function consistent with an oncogenic role, these four genes showed a strong correlation between amplification and overexpression and are therefore the best candidate driver oncogenes at 8p12 [7].
• We report that recruitment of BRFU to the TATA-box of these promoters is TATA-binding protein (TBP)-dependent [1].
• The amino acid sequences of two tryptic peptides derived from HPLC-purified heavier BRF-2 isoform were determined to be YLAIAPPIIK and ALYYLQIHPQELR [2].

Associations of BRF2 with chemical compounds

• Two other short-chain fatty acids, propionate and acetate, have no detectable effects on BRF1 or BRF2 transcription [8].

Physical interactions of BRF2

• The core domain of TBP is sufficient for BRFU.TBP.DNA complex formation and for interaction with BRFU off the template [1].

Regulatory relationships of BRF2

• TBP deactivates this negative mechanism through protein-protein contacts with both BRFU and hB", which may then promote their cooperative binding to form TFIIIB-alpha [6].

Analytical, diagnostic and therapeutic context of BRF2

• By gel mobility shift assay, we have identified a rat liver nuclear protein (BRF-2) which binds to the distal element (-128 to -85) of the apoB gene [9].
• In this paper we report the isolation of two isoforms of BRF-2 by further purification using high-performance liquid chromatography [2].
• Anti-peptide antisera raised against two synthetic peptides of XAP-1 recognized a approximately 120-kDa polypeptide band in both BRF-2 isoforms in a western blot analysis [2].

References