A TAF4-homology domain from the corepressor ETO is a docking platform for positive and negative regulators of transcription

Yufeng Wei, Shaohua Liu, Jörn Lausen, Christopher Woodrell, Seongeun Cho, Nikolaos Biris, Naohiro Kobayashi, Yu Wei, Shigeyuki Yokoyama, Milton H. Werner

Research output: Contribution to journalArticle

34 Scopus citations

Abstract

The eight twenty-one protein, ETO, is implicated in 12%-15% of acute human leukemias as part of a gene fusion with RUNX1 (also called AML1). Of the four ETO domains related to Drosophila melanogaster Nervy, only two are required to induce spontaneous myeloid leukemia upon transplantation into the mouse. One of these domains is related in sequence to TAF4, a component of TFIID. The structure of this domain, ETO-TAFH, is similar to yeast Rpb4 and to Escherichia coli σ70; it is the first TAF-related protein with structural similarity to the multisubunit RNA polymerases. Overlapping surfaces of ETO-TAFH interact with an autonomous repression domain of the nuclear receptor corepressor N-CoR and with a conserved activation domain from the E-box family of transcription factors. Thus, ETO-TAFH acts as a structural platform that can interchange negative and positive coregulatory proteins to control transcription.

Original languageEnglish (US)
Pages (from-to)653-661
Number of pages9
JournalNature Structural and Molecular Biology
Volume14
Issue number7
DOIs
StatePublished - Jul 1 2007

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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    Wei, Y., Liu, S., Lausen, J., Woodrell, C., Cho, S., Biris, N., Kobayashi, N., Wei, Y., Yokoyama, S., & Werner, M. H. (2007). A TAF4-homology domain from the corepressor ETO is a docking platform for positive and negative regulators of transcription. Nature Structural and Molecular Biology, 14(7), 653-661. https://doi.org/10.1038/nsmb1258