Abstract
The E2F1 transcription factor has a well-characterized activation domain at its C terminus and the E1A protein has a recently defined activation domain at its N terminus. Here we show that these activation domains are highly related in sequence. The sequence homology reflects, at least partly, the conservation of common binding sites for the RB and CBP/p300 proteins, which are preserved in the same relative order along E2F1 and E1A. Furthermore, the interaction of RB and CBP with these two activation domains results in the same functional consequences: RB represses both activation domains, whereas CBP stimulates them. We conclude that the activation domains of E1A(12s) and E2F1 belong to a novel functional class, characterized by specific protein binding sites. The implication of this conservation with respect to E1A-induced stimulation of E2F activity is discussed.
MeSH Terms
Adenovirus E1A Proteins/chemistry,metabolism
Amino Acid Sequence
Binding Sites
Bone Neoplasms/pathology
CREB-Binding Protein
Carrier Proteins
Cell Cycle Proteins
DNA-Binding Proteins
E2F Transcription Factors
E2F1 Transcription Factor
Humans
Molecular Sequence Data
Mutagenesis, Site-Directed
Nuclear Proteins/metabolism
Osteosarcoma/pathology
Promoter Regions, Genetic
Protein Binding
Recombinant Fusion Proteins/biosynthesis
Retinoblastoma Protein/metabolism
Retinoblastoma-Binding Protein 1
Sequence Homology, Amino Acid
Structure-Activity Relationship
Trans-Activators
Transcription Factor DP1
Transcription Factors/chemistry,metabolism
Tumor Cells, Cultured
Chemicals
Adenovirus E1A Proteins
Carrier Proteins
Cell Cycle Proteins
DNA-Binding Proteins
E2F Transcription Factors
E2F1 Transcription Factor
E2F1 protein, human
Nuclear Proteins
Recombinant Fusion Proteins
Retinoblastoma Protein
Retinoblastoma-Binding Protein 1
Trans-Activators
Transcription Factor DP1
Transcription Factors
CREB-Binding Protein
CREBBP protein, human
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Trouche D
Wellcome/Cancer Research Campaign Institute, University of Cambridge, United Kingdom.
Kouzarides T
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