Abstract
A kinase activity can be immunoprecipitated in a complex that includes adeno virus E1A proteins. In vitro, this activity phosphorylated other E1A-associated proteins, as well as added E1A and histone H1 proteins. The E1A-associated kinase activity was cleared from extracts with an antibody to cyclin A, but not with antibody to cyclin B. The formation of a complex that included the kinase activity required amino acids 30-60 and 122-129 on the E1A proteins, sequences needed for association of E1A proteins with cyclin A and the retinoblastoma protein and implicated in control of cell growth. The complex of E1A-associated proteins included a 33-kDa ATP-binding protein, similar in size to a cyclin A-associated cdc2 kinase family member. Sucrose gradient analysis revealed two distinct E1A-containing complexes with the kinase activity. We suggest that E1A proteins may affect cellular proliferation by interacting with a member of the cdc2 kinase family and thereby influencing its activity.
Original language | English (US) |
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Pages (from-to) | 11143-11147 |
Number of pages | 5 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Volume | 88 |
Issue number | 24 |
State | Published - 1991 |
All Science Journal Classification (ASJC) codes
- General
Keywords
- Cyclin A
- E1A-associated kinase
- p33 kinase