ETO, a Target of t(8;21) in Acute Leukemia, Interacts with the N-CoR and mSin3 Corepressors

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Molecular and Cellular Biology, December 1998, p. 7176-7184, Vol. 18, No. 12
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

ETO, a Target of t(8;21) in Acute Leukemia, Interacts with the N-CoR and mSin3 Corepressors

Bart Lutterbach,¹^,² Jennifer J. Westendorf,¹^,² Bryan Linggi,¹^,² Andrea Patten,¹^,² Mariko Moniwa,³ James R. Davie,³ Khanh D. Huynh,⁴ Vivian J. Bardwell,⁴^,⁵ Robert M. Lavinsky,⁶ Michael G. Rosenfeld,⁶^,⁷ Christopher Glass,⁷ Edward Seto,⁸ and Scott W. Hiebert¹^,²^,^*

Department of Biochemistry¹ and Vanderbilt Cancer Center,² Vanderbilt University School of Medicine, Nashville, Tennessee 37232; Department of Biochemistry and Molecular Biology, University of Manitoba, Winnipeg, Manitoba R3E 0W3, Canada³; Biochemistry, Molecular Biology and Biophysics Graduate Program⁴ and Department of Biochemistry, Institute of Human Genetics and Cancer Center,⁵ University of Minnesota, Minneapolis, Minnesota 55455; Howard Hughes Medical Institute⁶ and Department of Medicine, School of Medicine,⁷ University of California, San Diego, La Jolla, California 92093-0648; and H. Lee Moffitt Cancer Center and Research Institute, University of South Florida, Tampa, Florida 33612⁸

Received 16 July 1998/Returned for modification 18 August 1998/Accepted 27 August 1998

t(8;21) is one of the most frequent translocations associated with acute myeloid leukemia. It produces a chimeric protein,acute myeloid leukemia-1 (AML-1)-eight-twenty-one (ETO), thatcontains the amino-terminal DNA binding domain of the AML-1 transcriptionalregulator fused to nearly all of ETO. Here we demonstrate thatETO interacts with the nuclear receptor corepressor N-CoR, themSin3 corepressors, and histone deacetylases. Endogenous ETO alsocosediments on sucrose gradients with mSin3A, N-CoR, and histonedeacetylases, suggesting that it is a component of one or morecorepressor complexes. Deletion mutagenesis indicates that ETOinteracts with mSin3A independently of its association with N-CoR.Single amino acid mutations that impair the ability of ETO tointeract with the central portion of N-CoR affect the abilityof the t(8;21) fusion protein to repress transcription. Finally,AML-1/ETO associates with histone deacetylase activity and a histonedeacetylase inhibitor impairs the ability of the fusion proteinto repress transcription. Thus, t(8;21) fuses a component of acorepressor complex to AML-1 to represstranscription.

^* Corresponding author. Mailing address: Department of Biochemistry, Vanderbilt Cancer Center, Vanderbilt University Schoolof Medicine, Medical Research Building II, Rm. 512, 23rd and Pierce,Nashville, TN 37232. Phone: (615) 936-3582. Fax: (615) 936-1790.E-mail: scott.hiebert{at}mcmail.vanderbilt.edu.

Molecular and Cellular Biology, December 1998, p. 7176-7184, Vol. 18, No. 12
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

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