Disease relevance of BRF1

• Melan-A- and EBV (BRF1) peptides were used and the frequency of antigen-specific CD8+ T cells was assessed using appropriate tetramers [1].
• RESULTS: The conjugate showed concentration-dependent toxicity for the following prostate cancer cell lines: BRF 41 T>DU145>PC-3>LNCaP, according to their LH receptor capacities [2].
• It was found that limbs with venous hypertension had a high skin resting blood flow (BRF) and an impaired veno-arteriolar reflex (VR) [3].
• There was a marked improvement in both BRF and VR after elastic compression for three weeks and an association between this improvement and the rate of healing of the leg ulcers [3].

Psychiatry related information on BRF1

• The BRF national prevalence estimate of chronic heavier drinking is 8.7 percent, equivalent to the 1979 National Institute on Alcoholism and Alcohol Abuse (NIAAA) estimate of 9 percent [4].

High impact information on BRF1

• S92 phosphorylation of BRF1 did not impair ARE binding, but induced complex formation with the scaffold protein 14-3-3 [5].
• Butyrate response factor (BRF1) belongs to the Tis11 family of CCCH zinc-finger proteins, which bind to mRNAs containing an AU-rich element (ARE) in their 3' untranslated region and promote their deadenylation and rapid degradation [5].
• Brf1 is hyperphosphorylated in metaphase-arrested cells, but remains associated with promoters in condensed chromosomes, along with TBP [6].
• By use of small interfering (si)RNA, independent evidence for an active role of BRF1 in mRNA degradation was obtained [7].
• Mutant slowC carries frame-shift mutations in both BRF1 alleles, whereas slowB with intermediate decay kinetics is heterozygous [7].

Biological context of BRF1

• Elevated expression of BRF1 decreased the level of the human inhibitor of apoptosis protein-2 (cIAP2) and increased the caspase-3 activity in HNSCC cells [8].
• Our initial data demonstrated that the immediate-early gene butyrate response factor 1 ( BRF1) was upregulated in HTLV-1-infected cells [9].
• BRF bound to TBP-DNA through the nonconserved C-terminal region and required 15 bp downstream of the TATA box and as little as 1 bp upstream of the TATA box for stable complex formation [10].
• The abundance of both TBP and BRF decreases during F9 cell differentiation [11].
• In this paper an epidemiological model with realistic demography is used to investigate the impact of the non-equilibrium conditions typical of the transition to sustained below replacement fertility (BRF) recently observed in a number of western countries, upon the transmission dynamics of measles [12].

Anatomical context of BRF1

• The proximal element (-84 to -70) acts as a positive element in both these cell lines, and two rat liver nuclear proteins, BRF-1 and C/EBP, bind to two overlapping sites (-84 to -60 and -70 to -50, respectively) [13].

Associations of BRF1 with chemical compounds

• Mutation of both serines to alanine uncouples BRF1 from PKB regulation, leading to constitutive mRNA decay even in the presence of stabilizing signals [14].
• These findings demonstrate that BRF1 expression enhanced cisplatin sensitivity in HNSCC cells by reducing the levels of cIAP2 mRNA [8].
• Hydroxyl radical footprinting of TFIIIB complexes and modeling the results to the TBP-DNA structure suggest that BRF and B" surround TBP on both faces of the TBP-DNA complex and provide an explanation for the exceptional stability of this complex [10].
• The adsorption of some textile dyes by diatomite was investigated using Sif Blau BRF (SB), Everzol Brill Red 3BS (EBR), and Int Yellow 5GF (IY) [15].

Regulatory relationships of BRF1

• BRF1 Protein Turnover and mRNA Decay Activity Are Regulated by Protein Kinase B at the Same Phosphorylation Sites [14].

Other interactions of BRF1

• Using immunopurified complexes containing the cloned hBRFs, we show that while hBRF1 functions at the 5S, VA1, 7SL and EBER2 promoters, a different variant, hBRF2, is required at the human U6 promoter [16].
• Alternatively spliced hBRF variants function at different RNA polymerase III promoters [16].
• The C-terminal half of TFIIIB90 contains a high-mobility-group protein 2 (HMG2)-related domain and interacts strongly with TBP [17].
• In addition, immunoprecipitation analyses demonstrate that substantial and similar molar amounts of TATA-binding protein (TBP) and TFIIIB90 can weakly associate with PTF at low salt conditions, but this association is dramatically reduced at high salt concentrations [18].
• Three complementary mechanisms may therefore allow high-risk HPV to stimulate production of tRNA and 5S rRNA: E6-mediated removal of p53; E7-mediated neutralization of RB; and induction of Brf1 [19].

References