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 Blood, 9 April 2009, Vol. 113, No. 15, pp. 3558-3567.
Prepublished online as a Blood First Edition Paper on February 9, 2009; DOI 10.1182/blood-2008-06-161307.

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MYELOID NEOPLASIA

Structure of the AML1-ETO eTAFH domain–HEB peptide complex and its contribution to AML1-ETO activity

Sangho Park1, Wei Chen2, Tomasz Cierpicki1, Marco Tonelli3, Xiongwei Cai4, Nancy A. Speck4, and John H. Bushweller1,5

1 Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville; 2 Department of Biochemistry, Dartmouth Medical School, Hanover, NH; 3 National Magnetic Resonance Facility at Madison, Biochemistry Department, University of Wisconsin-Madison; 4 Abramson Family Cancer Research Institute and Department of Cell and Developmental Biology, University of Pennsylvania, Philadelphia; and 5 Department of Chemistry, University of Virginia, Charlottesville

AML1-ETO is the chimeric protein product of the t(8;21) in acute myeloid leukemia. The ETO portion of the fusion protein includes the eTAFH domain, which is homologous to several TATA binding protein–associated factors (TAFs) and interacts with E proteins (E2A and HEB). It has been proposed that AML1-ETO–mediated silencing of E protein function might be important for t(8;21) leukemogenesis. Here, we determined the solution structure of a complex between the AML1-ETO eTAFH domain and an interacting peptide from HEB. On the basis of the structure, key residues in AML1-ETO for HEB association were mutated. These mutations do not impair the ability of AML1-ETO to enhance the clonogenic capacity of primary mouse bone marrow cells and do not eliminate its ability to repress proliferation or granulocyte differentiation. Therefore, the eTAFH-E protein interaction appears to contribute relatively little to the activity of AML1-ETO.


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