The involvement of the histone fold motifs in the mutual interaction between human TAF(II)80 and TAF(II)22.
The TATA box-binding factor TFIID mediates transcriptional regulation through interactions with various regulatory factors and putative participation in reconfiguration of nucleosomes, utilizing its components, which include TATA box-binding protein (TBP) and TBP-associated factors (TAFs). Our and other previous studies have elucidated that there exist histone-similar TAFs. Studies on TAFs similar to histone H3 and H4 have revealed their biochemical and structural similarities to the corresponding histones. However, the existence of histone-like interactions involving the other TAFs is still ambiguous. Here we report the analyses with a two-hybrid system of the mutually interacting regions between hTAF(II)80 and hTAF(II)22, which resemble histone H4 and H2B, respectively. The results demonstrate the indispensability of the histone fold motifs of these two TAFs for mutual interaction. Together with earlier biochemical or structural studies, the present results suggest the presence of a histone octamer-like partial TAF complex and its involvement in transcription from chromatin templates.
Bando
M
M
Department of Cellular Biology, Institute of Molecular and Cellular Biosciences, The University of Tokyo, Bunkyo-ku.
Ijuin
S
S
Hasegawa
S
S
Horikoshi
M
M
D006657:Histones / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D017510:Protein Folding; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D035381:TATA-Binding Protein Associated Factors; D014157:Transcription Factors / Q000378:metabolism*
D006657:Histones; D011993:Recombinant Fusion Proteins; C084977:TAF6 protein, human; D035381:TATA-Binding Protein Associated Factors; D014157:Transcription Factors