Adenovirus E1A is associated with a serine/threonine protein kinase.

Abstract

The adenovirus E1A proteins form stable protein complexes with a number of cellular proteins, including cyclin A and the product of the retinoblastoma susceptibility gene. We have been interested in learning about the function of proteins associated with E1A and therefore looked for an enzymatic activity present in E1A complexes. We found a serine/threonine kinase activity that phosphorylates two proteins bound to E1A, the 107- and 130-kDa (107K and 130K) proteins. The kinase also phosphorylates histone H1 added as an exogenous substrate. The kinase activity is cell cycle regulated, being most active in S and G2/M-phase cells. The timing of phosphorylation of the 107K protein in vitro correlates with the phosphorylation pattern of the 107K protein in vivo. A variety of genetic and immunochemical approaches indicate that the activity is probably not due to the E1A-associated 300K, 130K, 107K, or pRB protein. Although we have not established the identity of the kinase, we present evidence that the kinase activity is consistent with phosphorylation by p34cdc2 or a related kinase.

• Authors: C H Herrmann, L K Su, E Harlow
• Journal: Journal of virology (J Virol) Vol. 65 Issue 11 Pg. 5848-59 (Nov 1991) ISSN: 0022-538X [Print] United States
• PMID: 1833561 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Adenovirus Early Proteins
• Amino Acids
• Antigen-Antibody Complex
• Oncogene Proteins, Viral
• Phosphopeptides
• Transcription Factors
• Protein Kinases
• Protein Serine-Threonine Kinases
• CDC2 Protein Kinase

Topics

• Adenoviridae (physiology)
• Adenovirus Early Proteins
• Amino Acids (analysis)
• Antigen-Antibody Complex (analysis)
• Binding Sites
• CDC2 Protein Kinase (metabolism)
• Cell Line
• Chromosome Deletion
• HeLa Cells
• Humans
• Oncogene Proteins, Viral (genetics, metabolism)
• Peptide Mapping
• Phosphopeptides (isolation & purification)
• Protein Binding
• Protein Kinases (metabolism)
• Protein Serine-Threonine Kinases
• Transcription Factors (metabolism)