Nucleic Acids Research Advance Access originally published online on September 7, 2007
Nucleic Acids Research 2007 35(18):6137-6149; doi:10.1093/nar/gkm656
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Nucleic Acids Research, 2007, Vol. 35, No. 18 6137-6149
© 2007 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 |
Tip60 functions as a potential corepressor of KLF4 in regulation of HDC promoter activity
1Division of Digestive and Liver Diseases, Department of Medicine, Columbia University Medical Center, New York, NY 10032, USA, 2Department of General Surgery, Union Hospital Tongji Medical College, Wuhan 430022, China and 3Department of Pediatrics/Department of Cancer Biology, University of Massachusetts Medical Center, Worcester, MA 01605, USA
*To whom correspondence should be addressed. Tel: +1 212 851 4587; Fax: +1 212851 4590; Email: wa2108{at}columbia.edu
Received June 4, 2007. Revised August 7, 2007. Accepted August 7, 2007.
KLF4 is a transcription factor that is highly expressed in the gastrointestinal tract. Previously we have demonstrated that KLF4 represses HDC promoter activity in a gastric cell line through both an upstream Sp1 binding GC box and downstream gastrin responsive elements. However, the mechanism by which KLF4 inhibits HDC promoter is not well defined. In the current study, by using yeast two-hybrid screening, Tip60 was identified as a KLF4 interacting protein. Further coimmunoprecipitation and functional reporter assays support the interaction between these two proteins. In addition, Tip60 and HDAC7, previously shown to interact with each other and repress transcription, inhibited HDC promoter activity in a dose-dependent fashion. Consistently, knock down of Tip60 or HDAC7 gene expression by specific shRNA increased endogenous HDC mRNA level. Co-immunoprecipitation assays showed that HDAC7 was pulled down by KLF4 and Tip60, suggesting that these three proteins form a repressive complex. Further chromatin immuno-precipitation indicated that all three proteins associated with HDC promoter. Two-hour gastrin treatment, known to activate HDC gene expression, significantly decreased the association of KLF4, Tip60 and HDAC7 with HDC promoter, suggesting that gastrin activates HDC gene expression at least partly by decreasing the formation of KLF4/Tip60/HDAC7 repressive complexes at the HDC promoter.
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