Nucleic Acids Research Advance Access originally published online on December 7, 2006
Nucleic Acids Research 2007 35(1):175-185; doi:10.1093/nar/gkl1034
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Nucleic Acids Research, 2007, Vol. 35, No. 1 175-185
© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Molecular Biology |
Functional interaction between the homeoprotein CDX1 and the transcriptional machinery containing the TATA-binding protein
INSERM, U682 and University Louis Pasteur Strasbourg, France 1 CNRS UMR7104, IGBMC and University Louis Pasteur Illkirch, France
*To whom correspondence should be addressed at INSERM U682, 3 Avenue Molière, 67200 Strasbourg, France. Tel: +33 388 27 77 27; Fax: +33 388 26 35 38; Email: jean-noel.freund{at}inserm.u-strasbg.fr
Received April 3, 2006. Revised September 29, 2006. Accepted November 7, 2006.
We have previously reported that the CDX1 homeoprotein interacts with the TATA-box binding protein (TBP) on the promoter of the glucose-6-phosphatase (G6Pase) gene. We show here that CDX1 interacts with TBP via the homeodomain and that the transcriptional activity additionally requires the N-terminal domain upstream of the homeodomain. CDX1 interacting with TBP is connected to members of the TFIID and Mediator complexes, two major elements of the general transcriptional machinery. Transcription luciferase assays performed using an altered-specificity mutant of TBP provide evidence for the functionality of the interaction between CDX1 and TBP. Unlike CDX1, CDX2 does not interact with TBP nor does it transactivate the G6Pase promoter. Swapping experiments between the domains of CDX1 and CDX2 indicate that, despite opposite functional effects of the homeoproteins on the G6Pase promoter, the N-terminal domains and homeodomains of both CDX1 and CDX2 have the intrinsic ability to activate transcription and to interact with TBP. However, the carboxy domains define the specificity of CDX1 and CDX2. Thus, intra-molecular interactions control the activity and partner recruitment of CDX1 and CDX2, leading to different molecular functions.
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