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Mol Cell Biol, July 1998, p. 3915-3925, Vol. 18, No. 7
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Multiple Functional Domains of AML1: PU.1 and C/EBPalpha Synergize with Different Regions of AML1

Martha S. Petrovick,1 Scott W. Hiebert,2 Alan D. Friedman,3 Christopher J. Hetherington,1 Daniel G. Tenen,1 and Dong-Er Zhang1 *

Division of Hematology/Oncology, Department of Medicine, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts1; Department of Biochemistry, Vanderbilt Cancer Center, Vanderbilt University School of Medicine, Nashville, Tennessee2; and Division of Pediatric Oncology, Johns Hopkins Oncology Center, Baltimore, Maryland3

Received 11 February 1998/Returned for modification 23 March 1998/Accepted 13 April 1998

Control elements of many genes are regulated by multiple activators working in concert to confer the maximal level of expression, but the mechanism of such synergy is not completely understood. The promoter of the human macrophage colony-stimulating factor (M-CSF) receptor presents an excellent model with which we can study synergistic, tissue-specific activation for two reasons. First, myeloid-specific expression of the M-CSF receptor is regulated transcriptionally by three factors which are crucial for normal hematopoiesis: PU.1, AML1, and C/EBPalpha . Second, these proteins interact in such a way as to demonstrate at least two examples of synergistic activation. We have shown that AML1 and C/EBPalpha activate the M-CSF receptor promoter in a synergistic manner. As we report here, AML1 also synergizes, and interacts physically, with PU.1. Detailed analysis of the physical and functional interaction of AML1 with PU.1 and C/EBPalpha has revealed that the proteins contact one another through their DNA-binding domains and that AML1 exhibits cooperative DNA binding with C/EBPalpha but not with PU.1. This difference in DNA-binding abilities may explain, in part, the differences observed in synergistic activation. Furthermore, the activation domains of all three factors are required for synergistic activation, and the region of AML1 required for synergy with PU.1 is distinct from that required for synergy with C/EBPalpha . These observations present the possibility that synergistic activation is mediated by secondary proteins contacted through the activation domains of AML1, C/EBPalpha , and PU.1.

* Corresponding author. Mailing address: Room 953, Harvard Institutes of Medicine, 77 Ave. Louis Pasteur, Boston, MA 02115. Phone: (617) 667-8930. Fax: (617) 667-3299. E-mail: dzhang{at}bidmc.harvard.edu.

Mol Cell Biol, July 1998, p. 3915-3925, Vol. 18, No. 7
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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