[HTML][HTML] The p400 complex is an essential E1A transformation target
Here, we report the identification of a new E1A binding protein complex that is essential for
E1A-mediated transformation. Its core component is a SWI2/SNF2-related, 400 kDa protein
(p400). Other components include the myc-and p/CAF-associated cofactor, TRRAP/PAF400,
the DNA helicases TAP54α/β, actin-like proteins, and the human homolog of the Drosophila
Enhancer of Polycomb protein. An E1A mutant, defective in p400 binding, is also defective in
transformation. Certain p400 fragments partially rescued this phenotype, underscoring the …
E1A-mediated transformation. Its core component is a SWI2/SNF2-related, 400 kDa protein
(p400). Other components include the myc-and p/CAF-associated cofactor, TRRAP/PAF400,
the DNA helicases TAP54α/β, actin-like proteins, and the human homolog of the Drosophila
Enhancer of Polycomb protein. An E1A mutant, defective in p400 binding, is also defective in
transformation. Certain p400 fragments partially rescued this phenotype, underscoring the …
Abstract
Here, we report the identification of a new E1A binding protein complex that is essential for E1A-mediated transformation. Its core component is a SWI2/SNF2-related, 400 kDa protein (p400). Other components include the myc- and p/CAF-associated cofactor, TRRAP/PAF400, the DNA helicases TAP54α/β, actin-like proteins, and the human homolog of the Drosophila Enhancer of Polycomb protein. An E1A mutant, defective in p400 binding, is also defective in transformation. Certain p400 fragments partially rescued this phenotype, underscoring the role of E1A-p400 complex formation in the E1A transforming process. Furthermore, E1A and c-myc each alter the subunit composition of p400 complexes, implying that physiological p400 complex formation contributes to transformation suppression.
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