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Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11143-7.

A protein kinase is present in a complex with adenovirus E1A proteins.

Author information

1
Howard Hughes Medical Institute, Department of Molecular Biology, Princeton University, NJ 08544-1014.

Abstract

A kinase activity can be immunoprecipitated in a complex that includes adenovirus 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.

PMID:
1837143
PMCID:
PMC53090
DOI:
10.1073/pnas.88.24.11143
[Indexed for MEDLINE]
Free PMC Article

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