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Molecular and Cellular Biology, October 2001, p. 6470-6483, Vol. 21, No. 19
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.19.6470-6483.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

ETO, a Target of t(8;21) in Acute Leukemia, Makes Distinct Contacts with Multiple Histone Deacetylases and Binds mSin3A through Its Oligomerization Domain

Joseph M. Amann,1,2 John Nip,1,2 David K. Strom,1,2,dagger Bart Lutterbach,1,2 Hironori Harada,3 Noel Lenny,3,4 James R. Downing,3 Shari Meyers,5 and Scott W. Hiebert1,2,*

Department of Biochemistry1 and Vanderbilt-Ingram Cancer Center,2 Vanderbilt University School of Medicine, Nashville, Tennessee 37232; Departments of Pathology3 and Tumor Cell Biology,4 St. Jude Children's Research Hospital, Memphis, Tennessee 38105; and Department of Biochemistry and Molecular Biology and the Feist-Weiller Cancer Center, Louisiana State University Health Services Center, Shreveport, Louisiana 71130-39325

Received 26 February 2001/Returned for modification 5 April 2001/Accepted 26 June 2001

t(8;21) and t(16;21) create two fusion proteins, AML-1-ETO and AML-1-MTG16, respectively, which fuse the AML-1 DNA binding domain to putative transcriptional corepressors, ETO and MTG16. Here, we show that distinct domains of ETO contact the mSin3A and N-CoR corepressors and define two binding sites within ETO for each of these corepressors. In addition, of eight histone deacetylases (HDACs) tested, only the class I HDACs HDAC-1, HDAC-2, and HDAC-3 bind ETO. However, these HDACs bind ETO through different domains. We also show that the murine homologue of MTG16, ETO-2, is also a transcriptional corepressor that works through a similar but distinct mechanism. Like ETO, ETO-2 interacts with N-CoR, but ETO-2 fails to bind mSin3A. Furthermore, ETO-2 binds HDAC-1, HDAC-2, and HDAC-3 but also interacts with HDAC-6 and HDAC-8. In addition, we show that expression of AML-1-ETO causes disruption of the cell cycle in the G1 phase. Disruption of the cell cycle required the ability of AML-1-ETO to repress transcription because a mutant of AML-1-ETO, Delta 469, which removes the majority of the corepressor binding sites, had no phenotype. Moreover, treatment of AML-1-ETO-expressing cells with trichostatin A, an HDAC inhibitor, restored cell cycle control. Thus, AML-1-ETO makes distinct contacts with multiple HDACs and an HDAC inhibitor biologically inactivates this fusion protein.

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

dagger Present address: Department of Biology, University of South Carolina, Aiken, SC 29801.

Molecular and Cellular Biology, October 2001, p. 6470-6483, Vol. 21, No. 19
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.19.6470-6483.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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