The functional interaction between HMGA1 and the estrogen receptor requires either the N- or the C-terminal domain of the receptor

被引:4
|
作者
Massaad-Massade, L
Tacine, R
Dulauroy, S
Reeves, R
Barouki, R
机构
[1] Univ Paris 05, Mol Toxicol Lab, INSERM, U 490, F-75270 Paris, France
[2] Washington State Univ, Sch Mol Biosci, Dept Biochem, Pullman, WA 99164 USA
[3] Hop Georges Pompidou, Serv Biochim, F-75015 Paris, France
来源
FEBS LETTERS | 2004年 / 559卷 / 1-3期
关键词
high mobility group; estrogen receptor domain; DNA binding; transactivation;
D O I
10.1016/S0014-5793(04)00032-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We have previously shown that HMGA1 enhances the transcriptional activity of promoters containing the estrogen response element (ERE) and increases binding of the estrogen receptor (ER) to ERE. Herein, we have assessed the transcriptional activity and ERE-binding ability of deleted ER fragments in absence or in presence of HMGA1. The HMGA1 protein stimulated binding and transcriptional activity by a factor of about 2-fold compared to the wild-type ER and both the Nand C-terminal ER deleted domains, but had no effect when both domains were deleted. These data show that HMGA1 cooperates with either the N- or the C-terminal transcriptional activation domain of the ER. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:89 / 95
页数:7
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