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Homeodomain interaction with the beta subunit of the general transcription factor TFIIE

Homeodomain-containing proteins play a crucial role as transcriptional regulators in the process of cell differentiation. The homeodomain performs a dual function in this regard, acting as a DNA binding domain and participating in protein-protein interactions that enhance DNA binding specificity or...

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Bibliographic Details
Published in:The Journal of biological chemistry 1996-08, Vol.271 (35), p.20993-20996
Main Authors: Zhu, A, Kuziora, M.A
Format: Article
Language:English
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Summary:Homeodomain-containing proteins play a crucial role as transcriptional regulators in the process of cell differentiation. The homeodomain performs a dual function in this regard, acting as a DNA binding domain and participating in protein-protein interactions that enhance DNA binding specificity or regulatory activity. Here we describe a homeodomain class-specific interaction with the beta subunit of the general transcription factor TFIIE. We show that the Antennapedia and Abdominal-B homeodomains bind to TFIIEbeta, but the even-skipped homeodomain does not. Using a two-hybrid assay performed in cultured cells, we demonstrate that the homeodomain-TFIIEbeta interaction occurs in vivo. The Abdominal-B homeodomain is shown to activate transcription in vitro, and this activation can be blocked with anti-TFIIEbeta antibody without affecting basal transcription levels. Together with published data demonstrating an interaction between proteins containing even-skipped class homeodomains and the TATA-binding protein (Um, M., Li, C., and Manley, J.L. (1995) Mol. Cell. Biol. 15, 5007-5016; Zhang, H., Catron, K. M., and Abate-Shen, C. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 1764-1769), these results suggest various homeodomain containing proteins interact with different general transcription factors, an observation that may have important implications for transcriptional regulation
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.271.35.20993