Identification of a highly conserved domain that suppresses the DNA-binding domain-DNA interactions in the androgen receptor.
- Author:
Guo-zhen LIU
1
;
Hua WANG
;
Zheng-xing WANG
Author Information
1. Department of Infectious Diseases, Xiangya Hospital, Central South University, Changsha 410008, China. guozhenliu@yahoo.com
- Publication Type:Journal Article
- MeSH:
Adult;
DNA;
metabolism;
DNA-Binding Proteins;
chemistry;
genetics;
Gene Expression Regulation;
Humans;
Male;
Mutation;
Receptors, Androgen;
chemistry;
genetics;
Response Elements;
Transcriptional Activation;
Transfection
- From:
Journal of Central South University(Medical Sciences)
2005;30(4):394-398
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVE:To determine the gene regulation of androgen receptor (AR).
METHODS:Gel shift assay, protein-protein pull down assay, western blot and technique of site-directed mutagenesis were used to study the gene regulation of AR.
RESULTS:The N terminal of AR contained an inhibitory domain located in an 81-amino acid segment lying upstream of the DNA-binding domain (DBD). The inhibitory domain interacted directly with DBD and repressed DBD binding to the ARE. Mutations of the conserved amino acid residues (K520E and R538E) within the inhibitory domain decreased its inhibiting ability in vitro and increased AR trans-activation in vivo.
CONCLUSION:These data demonstrated the existence of a novel inhibitory domain in the N-terminal part of AR, which might play important role in the regulation of AR trans-activation.
