J. Biochem, 2004, Vol. 135, No. 2 217-223
© 2004 The Japanese Biochemical Society
MOLECULAR BIOLOGY |
Identification of the Transactivating Region of the Homeodomain Protein, Hex
1 Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa-ku, Nagoya 464-8601; and 2 Division of Stem Cell Regulation Research, Osaka University Medical School, Suita, Osaka 565-0871
The homeodomain-containing protein Hex acts as an activator as well as a repressor of transcription in animals. While its repression domain has been mapped to the amino-terminal region, the activation domain has never been identified. Here, we show that the homeodomain and the acidic carboxyl-terminal region are necessary for full activation of the sodium-dependent bile acid cotransporter gene promoter in a cell type-independent manner, suggesting that the carboxyl-terminal region comprising residues 197 to 271 functions as the activation domain. In addition, we observed that a Hex mutant without this activation domain acts as a dominant-negative mutant as to the transactivating function of Hex.
* To whom correspondence should be addressed. Fax: +81-52-789-4121, E-mail: tnoguchi{at}agr.nagoya-u.ac.jp
![]()
CiteULike
Connotea
Del.icio.us What's this?
This article has been cited by other articles:
![]() |
A. Soufi, P. Noy, M. Buckle, A. Sawasdichai, K. Gaston, and P.-S. Jayaraman CK2 phosphorylation of the PRH/Hex homeodomain functions as a reversible switch for DNA binding Nucleic Acids Res., June 1, 2009; 37(10): 3288 - 3300. [Abstract] [Full Text] [PDF] |
||||
