In vitro association between the Jun protein family and the general transcription factors, TBP and TFIIB

C. C. Franklin, A. V. McCulloch, A. S. Kraft

Research output: Contribution to journalArticle

33 Scopus citations

Abstract

Transcriptional activator proteins interact with the general transcription factors TATA-binding protein (TBP), TFIIB and/or other TBP-associated factors (TAFs). Using affinity chromatography we demonstrate that members of the Jun family of transcriptional activators interact with both TBP and TFIIB in vitro. TBP binds to both the N-terminal activation domain and C-terminal bZIP regions of c-Jun, whereas TFIIB binds to only the c-Jun bZIP domain. This interaction requires the dimerization of the Jun protein. The ability of the N-terminal activation domains of c-Jun, JunB, JunD and v-Jun to interact with TBP in vitro correlates with their transcriptional activity in vivo. Domain mapping experiments indicate that c-Jun interacts with the conserved C-terminus of TBP. Studies using a set of TFIIB inframe deletion mutants demonstrate that C-terminal amino acids 178-201 and 238-316 play an important role in modulating the interaction between TFIIB and c-Jun. Although phosphorylation of the c-Jun N-terminal activation domain stimulates c-Jun transcriptional activity in vitro, it has no effect on the ability of c-Jun to intersct with either TBP or TFIIB in vitro. These data suggest that the Jun family of activator proteins may activate transcription by interacting with the general transcription factors TBP and TFIIB.

Original languageEnglish (US)
Pages (from-to)967-974
Number of pages8
JournalBiochemical Journal
Volume305
Issue number3
DOIs
StatePublished - Jan 1 1995
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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