High impact information on Taf5

• Purified recombinant dTAFII80 is unable to bind TBP directly or to interact strongly with the C-terminal domain of dTAFII250 (delta N250) [1].
• We propose a model in which Esc is recruited by gap proteins both to act as a corepressor that competes with the TAFII80 coactivator to block transcription and also to mediate the transition to permanent repression by Polycomb-group proteins [2].
• Molecular cloning and expression of the 32-kDa subunit of human TFIID reveals interactions with VP16 and TFIIB that mediate transcriptional activation [3].
• To further understand the role of the 85-kDa TFIID subunit (p85), we have cloned the corresponding cDNA with a probe based on an amino acid sequence of the purified protein [4].
• Yeast TFIID comprises the TATA binding protein and 14 TBP-associated factors (TAF(II)s), nine of which contain histone-fold domains (HFDs) [5].

Biological context of Taf5

• PI3K_68D has the potential to bind to signalling molecules containing SH3 domains, lacks p85-adaptor-binding sequences, has a Ca(2+)-independent phospholipid-binding domain and displays a restricted in vitro substrate specificity, so it could define a novel signal transduction pathway [6].
• The resulting TFIID complex supports normal cell growth, but it is unable to mediate Sp1-dependent activation [7].
• The droPIK57 gene encodes a protein containing two SH2 domains with significant sequence homology to those in p85 and p55 [8].

Analytical, diagnostic and therapeutic context of Taf5

• Sequence analysis reveals that dTAFII80 contains several copies of the WD40 (beta-transducin) repeat [1].
• Molecular cloning, expression, and characterization of the Drosophila 85-kilodalton TFIID subunit [4].

References