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  An extended winged helix domain in general transcription factor E/IIEα.

Meinhart, A., Blobel, J., & Cramer, P. (2003). An extended winged helix domain in general transcription factor E/IIEα. The Journal of Biological Chemistry, 278(48), 48267-48274. doi:10.1074/jbc.M307874200.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-8643-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-C641-4
Genre: Journal Article

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 Creators:
Meinhart, A., Author
Blobel, J., Author
Cramer, P.1, Author              
Affiliations:
1Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

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 Abstract: Initiation of eukaryotic mRNA transcription requires melting of promoter DNA with the help of the general transcription factors TFIIE and TFIIH. Here we define a conserved and functionally essential N-terminal domain in TFE, the archaeal homolog of the large TFIIE subunit α. X-ray crystallography shows that this TFE domain adopts a winged helix-turn-helix (winged helix) fold, extended by specific α-helices at the N and C termini. Although the winged helix fold is often found in DNA-binding proteins, we show that TFE is not a typical DNA-binding winged helix protein, because its putative DNA-binding face shows a negatively charged groove and an unusually long wing, and because the domain lacks DNA-binding activity in vitro. The groove and a conserved hydrophobic surface patch on the additional N-terminal α-helix may, however, allow for interactions with other general transcription factors and RNA polymerase. Homology modeling shows that the TFE domain is conserved in TFIIEα, including the potential functional surfaces.

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Language(s): eng - English
 Dates: 2003-09-172003-11-28
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1074/jbc.M307874200
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Title: The Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 278 (48) Sequence Number: - Start / End Page: 48267 - 48274 Identifier: -