Transcription initiation factor TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. The complex includes TATA binding protein (TBP) and various TBP-associated factors (TAFS). TFIID is a RNA polymerase II-specific TATA-binding protein-associated factor (TAF) that is essential for viability.This group represents a transcription initiation factor TFIID subunit 1 (TAF1, also known as cell cycle gene 1 protein) [, , ]. This is the largest subunit and the core scaffold of the complex, contains Ser/Thr kinase domains which can autophosphorylate or transphosphorylate other transcription factors including TP53, GTF2A1 and GTF2F1 [, ], and has acetyltransferase activity towards histones H3 and H4 []. It is essential for progression of the G1 phase of the cell cycle [].
This entry represents a domain found in C terminus of Atg11. Proteins containing this domain include Taf1 and Atg11. In Schizosaccharomyces pombe (fission yeast) Taf1 (taz1 interacting factor) is part of the telomere cap complex. In Saccharomyces cerevisiae (baker's yeast) Atg11 is known to be involved in vacuolar targeting and peroxisome degradation [, ].
Transcription initiation factor TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. The complex includes TATA binding protein (TBP) and various TBP-associated factors (TAFS). TFIID is a RNA polymerase II-specific TATA-binding protein-associated factor (TAF) that is essential for viability.This group represents a transcription initiation factor TFIID subunit 1 (TAF1, also known as cell cycle gene 1 protein) [, , ]. This is the largest subunit and the core scaffold of the complex, contains Ser/Thr kinase domains which can autophosphorylate or transphosphorylate other transcription factors including TP53, GTF2A1 and GTF2F1 [, ], and has acetyltransferase activity towards histones H3 and H4 []. It is essential for progression of the G1 phase of the cell cycle [].This entry represents the histone acetyltransferase domain (HAT, formerly known as DUF3591) that is found centrally in the protein TAF1 from eukaryotes. This region is highly conserved from yeast to human. X-ray determination of the crystal structure show it has a compact architecture that consists of a winged helix (WH) domain that folds on top of a triple barrel and a C-terminal α-helical region. The WH domain has intrinsic DNA-binding activity [, , , ].
