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The p250 subunit of native TATA box-binding factor TFIID is the cell-cycle regulatory protein CCG1 Koji Hisatake*, Satoshi Hasegawa*, Ritsuko Takada*, Yoshihiro Nakatanl†, Masami Horikoshi*‡ & Robert G. Roeder*
*Laboratory of Biochemistry and Molecular Biology,
The Rockefeller University, New York, New York 10021, USA
†Laboratory of Molecular Biology, NINDS,
National Institutes of Health, Bethesda, Maryland 20892, USA
‡Present address: Institute of Applied Microbiology, University of Tokyo, Bunkyo-ku, Tokyo 113, Japan.
THE protein TFIID is a general transcription factor1 which initiates preinitiation complex assembly2–4 through direct interaction with the TATA promoter element5,6. It is a multisubunit complex containing a small TATA-binding polypeptide (TBP) and other TBP-associated factors (TAFs) ranging in size from about 30–250K (refs 7–10). Although native TFIID can mediate both activator-independent (basal) and activator-dependent transcription in reconstituted systems3,5,6, TBP itself can mediate only basal transcription11,12, even in cases where TBP or the general factor TFIIB are known to interact directly with transcriptional activators13–15. TFIID subunits other than TBP must therefore be essential cofactors, and thus potential targets for activators, consistent with earlier demonstrations that activators interact with TFIID (refs 3, 5, 16, 17). Here we show that the 250K subunit of TFIID is identical to a gene product previously implicated in progression through the late Gl phase of the cell cycle18,19. Part of p250 may thus serve a specific function in the activation of a subset of genes important for cell cycle progression.
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