[Determination of ETO interaction domain within nuclear receptor co-repressor].

Objective To determine the ETO interaction domain of nuclear receptor co repressor (N CoR) for abolishing the biological function of AML1 ETO. Methods Ten 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. Results It was shown that the co existance 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. Conclusion Two domains of N CoR that interact with two zinc fingers of ETO, and keep stable binding between the two proteins were identified.