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Transcriptional activity of the TFIIA four-helix bundle in vivo

✍ Scribed by Laurie A. Stargell; Ryan C. Ogg; Joshua N. Adkins; Mary M. Robinson; Kevin J. Lumb

Publisher: John Wiley and Sons
Year: 2001
Tongue: English
Weight: 182 KB
Volume: 43
Category: Article
ISSN: 0887-3585
DOI: 10.1002/1097-0134(20010501)43:2<227::aid-prot1033>3.0.co;2-c

No coin nor oath required. For personal study only.

✦ Synopsis

TFIIA contributes to transcription initiation by stabilizing the TBP-TATA interaction and by mediating the response to transcriptional activators and inhibitors. TFIIA contains a sixstranded ␤-sheet domain and a four-helix bundle. The ␤-domain makes functional contacts with DNA and TBP. The role of the four-helix bundle was investigated using a structure-based model of this domain (called 4HB). 4HB adopts a highly stable, helical fold, consistent with its structure in the context of TFIIA. Like TBP and other intact transcription factors, 4HB is able to activate transcription in vivo when artificially recruited to a promoter via a heterologous DNA-binding domain. Thus, in addition to making important contacts with TBP and DNA via the ␤-domain, TFIIA makes other specific, functional contacts with the transcriptional machinery via the four-helix bundle. Proteins 2001;43:227-232.

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