Abstract
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-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.
Conclusion:
Two domains of N-CoR that interact with two zinc fingers of ETO, and keep stable binding between the two proteins were identified.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites / genetics
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Humans
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Nuclear Proteins / chemistry
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism*
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Nuclear Receptor Co-Repressor 1
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Plasmids / genetics
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Protein Binding
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Proto-Oncogene Proteins / genetics
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Proto-Oncogene Proteins / metabolism*
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RUNX1 Translocation Partner 1 Protein
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Repressor Proteins / chemistry
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Repressor Proteins / genetics
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Repressor Proteins / metabolism*
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Transcription Factors / genetics
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Transcription Factors / metabolism*
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Transfection
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Two-Hybrid System Techniques
Substances
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NCOR1 protein, human
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Nuclear Proteins
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Nuclear Receptor Co-Repressor 1
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Proto-Oncogene Proteins
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RUNX1 Translocation Partner 1 Protein
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RUNX1T1 protein, human
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Recombinant Fusion Proteins
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Repressor Proteins
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Transcription Factors