Abstract:
:Transcription initiation factor TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. 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. The recombinant p85 interacts directly with both the TATA box-binding subunit (TFIID tau or TBP) and the 110-kDa subunit (p110) of TFIID, suggesting that p85 may play a role in helping to anchor p110 within the TFIID complex and, with other studies, that TFIID assembly and function may involve a concerted series of subunit interactions. Interestingly, the carboxy terminus of p85 contains eight of the WD-40 repeats found originally in the beta subunit of G proteins and more recently in other transcriptional regulatory factors. However, truncated p85 lacking all the WD-40 repeats maintained interactions with both TFIID tau and p110. These observations leave open the possibility of a distinct function for the WD-40 repeats, possibly in transducing signals by interactions with transcriptional regulators and/or other components of the basic transcriptional machinery.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
Kokubo T,Gong DW,Yamashita S,Takada R,Roeder RG,Horikoshi M,Nakatani Ydoi
10.1128/mcb.13.12.7859subject
Has Abstractpub_date
1993-12-01 00:00:00pages
7859-63issue
12eissn
0270-7306issn
1098-5549journal_volume
13pub_type
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