Determination of ETO interaction domain within nuclear receptor co-repressor.
- Author:
Min WANG
1
;
Changlai HAO
;
Kejing TANG
;
Haiyan XING
;
Zheng TIAN
;
Yi ZHANG
;
Jianxiang WANG
Author Information
- Publication Type:Journal Article
- MeSH: Binding Sites; genetics; Humans; Nuclear Proteins; chemistry; genetics; metabolism; Nuclear Receptor Co-Repressor 1; Plasmids; genetics; Protein Binding; Proto-Oncogene Proteins; genetics; metabolism; RUNX1 Translocation Partner 1 Protein; Recombinant Fusion Proteins; genetics; metabolism; Repressor Proteins; chemistry; genetics; metabolism; Transcription Factors; genetics; metabolism; Transfection; Two-Hybrid System Techniques
- From: Chinese Journal of Hematology 2002;23(12):621-623
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo determine the ETO-interaction domain of nuclear receptor co-repressor (N-CoR) for abolishing the biological function of AML1-ETO.
METHODSTen different regions of N-CoR (N-CoRYs) were generated by means of polymerase chain reaction (PCR), and cloned into yeast expression plasmid pGADGL to construct pGADGL/N-CoRYs. The yeast two-hybrid technique and X-gal staining were used to determine the binding between the 10 different regions of N-CoR and ETO.
RESULTSIt was shown that the co-existence of 988-1,126 and 1,551-1,803 amino acid residues of N-CoRY was the ETO-interaction domains required for the binding with ETO.
CONCLUSIONTwo domains of N-CoR that interact with two zinc fingers of ETO, and keep stable binding between the two proteins were identified.
