Determination of ETO interaction domain within nuclear receptor co-repressor / 中华血液学杂志

ABSTRACT

<p><b>OBJECTIVE</b>To determine the ETO-interaction domain of nuclear receptor co-repressor (N-CoR) for abolishing the biological function of AML1-ETO.</p><p><b>METHODS</b>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.</p><p><b>RESULTS</b>It 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.</p><p><b>CONCLUSION</b>Two domains of N-CoR that interact with two zinc fingers of ETO, and keep stable binding between the two proteins were identified.</p>