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The p400 Complex Is an Essential E1A Transformation Target
- Source :
- Cell. (3):297-307
- Publisher :
- Cell Press.
-
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.
- Subjects :
- Macromolecular Substances
Protein subunit
viruses
Amino Acid Motifs
Molecular Sequence Data
Mutant
General Biochemistry, Genetics and Molecular Biology
Proto-Oncogene Proteins c-myc
03 medical and health sciences
chemistry.chemical_compound
0302 clinical medicine
RUVBL2
Humans
Amino Acid Sequence
Cloning, Molecular
Enhancer
Adaptor Proteins, Signal Transducing
Sequence Deletion
030304 developmental biology
Adenosine Triphosphatases
0303 health sciences
biology
Biochemistry, Genetics and Molecular Biology(all)
Binding protein
DNA Helicases
Antibodies, Monoclonal
Nuclear Proteins
Helicase
Precipitin Tests
Molecular biology
Peptide Fragments
Cell biology
DNA-Binding Proteins
Molecular Weight
Protein Subunits
Transformation (genetics)
Cell Transformation, Neoplastic
chemistry
030220 oncology & carcinogenesis
Trans-Activators
biology.protein
Adenovirus E1A Proteins
DNA
HeLa Cells
Protein Binding
Transcription Factors
Subjects
Details
- Language :
- English
- ISSN :
- 00928674
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- Cell
- Accession number :
- edsair.doi.dedup.....8ea963a81dd6de9bc8a88d39ece71c0e
- Full Text :
- https://doi.org/10.1016/S0092-8674(01)00450-0