High impact information on BDF1

• Efficient deposition of H2A.Z is further promoted by a specific pattern of histone H3 and H4 tail acetylation and the bromodomain protein Bdf1, a component of the Swr1 remodeling complex that deposits H2A.Z [1].
• Our data also indicate that the in vivo binding of the transcription factor Bdf1 is associated with acetylation on most lysines but relative deacetylation on H4 lysine 16 [2].
• Deletion of Bdf1 or the Taf67 Bdf-interacting domain leads to defects in gene expression [3].
• The structural and functional similarities suggest that Bdf1 corresponds to the carboxy-terminal region of higher eukaryotic TAF(II)250 and that the interaction between TFIID and Bdf1 is important for proper gene expression [3].
• Bromodomain point mutations that block Bdf1 binding to histones disrupt transcription and reduce Bdf1 association with chromatin in vivo [4].

Biological context of BDF1

• We have selected multicopy extragenic suppressor genes, revealing that this phenotype can be suppressed by overdosing the transcription factors BDF1 and GAT1 in the yaf9Delta strain [5].
• Furthermore, yeast strain lacking the BDF1 gene shows the Spt phenotype that is shown also by the ASF1 gene disruptant, and a double-knockout strain of both genes shows synthetic lethality, indicating that ASF1 genetically interacts with bromodomains associated with yTFIID [6].
• In this report, genetic analysis indicated that the salt sensitivity of the BDF1 deletion mutant was suppressed by increased gene dosage of its homologous gene BDF2 [7].
• Surprisingly, deletion of BDF1 or a Bdf1 mutation that abolishes histone binding leads to transcriptional downregulation of genes located at heterochromatin-euchromatin boundaries [8].
• Representatives of the TFIID pathway include the TATA binding protein, TAF1, and Bdf1 [9].

Anatomical context of BDF1

• The data derived from assays for polyuridine-directed polyphenylalanine synthesis of isolated ribosomes demonstrated that the ID50 values obtained were consistent with the observed inhibition of whole cell protein synthesis inhibition for P-388 cells, as well as for BDF1 and DBA/2 liver cells [10].

Other interactions of BDF1

• The bromodomain-containing protein Bdf1p acts as a phenotypic and transcriptional multicopy suppressor of YAF9 deletion in yeast [5].
• Moreover, like Htz1 and Bdf1, the SWR-C promotes gene expression near silent heterochromatin [11].
• The findings suggest that Bdf1 blocks assembly, whereas Mot1 promotes disassembly of the transcription machinery [9].
• Biochemical experiments indicate that Bdf1 competes with the Sir2 deacetylase for binding to acetylated histone H4 [8].

Analytical, diagnostic and therapeutic context of BDF1

• Using a yeast two-hybrid assay we detected an interaction between the N-terminal region of histone H4 (amino acids 1--59) and a fragment of the bromodomain factor 1 protein (Bdf1p) (amino acids 304--571) that includes one of the two bromodomains of this protein [12].

References