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

T. Kleinberger, T. Shenk

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)11143-11147
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number24
DOIs
StatePublished - 1991

All Science Journal Classification (ASJC) codes

  • General

Keywords

  • E1A-associated kinase
  • cyclin A
  • p33(cdc2) kinase

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