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 TAP54alpha/beta, 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.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Adenosine Triphosphatases, Adenovirus E1A Proteins, Amino Acid Motifs, Amino Acid Sequence, Antibodies, Monoclonal, Cell Transformation, Neoplastic, Cloning, Molecular, DNA Helicases, DNA-Binding Proteins, Hela Cells, Humans, Macromolecular Substances, Molecular Sequence Data, Molecular Weight, Nuclear Proteins, Peptide Fragments, Precipitin Tests, Protein Binding, Protein Subunits, Proto-Oncogene Proteins c-myc, Sequence Deletion, Trans-Activators, Transcription Factors
Adaptor Proteins, Signal Transducing, Adenosine Triphosphatases, Adenovirus E1A Proteins, Amino Acid Motifs, Amino Acid Sequence, Antibodies, Monoclonal, Cell Transformation, Neoplastic, Cloning, Molecular, DNA Helicases, DNA-Binding Proteins, Hela Cells, Humans, Macromolecular Substances, Molecular Sequence Data, Molecular Weight, Nuclear Proteins, Peptide Fragments, Precipitin Tests, Protein Binding, Protein Subunits, Proto-Oncogene Proteins c-myc, Sequence Deletion, Trans-Activators, Transcription Factors
Cell
Date: Aug. 10, 2001
PubMed ID: 11509179
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