Adenovirus E1A is associated with a serine/threonine protein kinase

Herrmann, C. H., Su, L. K., Harlow, E. (November 1991) Adenovirus E1A is associated with a serine/threonine protein kinase. Journal of Virology, 65 (11). pp. 5848-5859. ISSN 0022-538x



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.

Item Type: Paper
Uncontrolled Keywords: retinoblastoma susceptibility gene region 1a proteins e1a proteins cell-cycle epithelial-cells osteo-sarcoma rb gene product transformation expression
Subjects: organism description > virus > adenovirus
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase
CSHL Authors:
Communities: CSHL labs > Stillman lab
Depositing User: Matt Covey
Date: November 1991
Date Deposited: 14 Jan 2016 17:57
Last Modified: 14 Jan 2016 17:57
PMCID: PMC250247
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