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| IDENTIFICATION OF AML-1 AND THE (8 21) TRANSLOCATION PROTEIN (AML-1/ETO) AS SEQUENCE-SPECIFIC DNA-BINDING PROTEINS - THE RUNT HOMOLOGY DOMAIN IS REQUIRED FOR DNA-BINDING AND PROTEIN-PROTEIN INTERACTIONS |
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| Author(s): MEYERS S, DOWNING JR, HIEBERT SW |
| Source: MOLECULAR AND CELLULAR BIOLOGY Volume: 13 Issue: 10 Pages: 6336-6345 Published: OCT 1993 |
| Times Cited: 357 References: 49 |
| Abstract: The AML1 gene on chromosome 21 is disrupted in the (8;2 1) (q22;q22) translocation associated with acute myelogenous leukemia and encodes a protein with a central 118-amino-acid domain with 69% homology to the Drosophila pair-rule gene, runt. We demonstrate that AML-1 is a DNA-binding protein which specifically interacts with a sequence belonging to the group of enhancer core motifs, TGT/cGGT. Electrophoretic mobility shift analysis of cell extracts identified two AML-1-containing protein-DNA complexes whose electrophoretic mobilities were slower than those of complexes formed with AML-1 produced in vitro. Mixing of in vitro-produced AML-1 with cell extracts prior to gel mobility shift analysis resulted in the formation of higher-order complexes. Deletion mutagenesis of AML-1 revealed that the runt homology domain mediates both sequence-specific DNA binding and protein-protein interactions. The hybrid product, AML-1/ETO, which results from the (8;21) translocation and retains the runt homology domain, both recognizes the AML-1 consensus sequence and interacts with other cellular proteins. |
| Document Type: Article |
| Language: English |
Addresses:
1. ST JUDE CHILDRENS HOSP, DEPT TUMOR CELL BIOL, MEMPHIS, TN 38105 USA
2. ST JUDE CHILDRENS HOSP, DEPT PATHOL, MEMPHIS, TN 38105 USA |
| Publisher: AMER SOC MICROBIOLOGY, 1325 MASSACHUSETTS AVENUE, NW, WASHINGTON, DC 20005-4171 |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology |
| IDS Number: LY424 |
| ISSN: 0270-7306 |
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