Cell cycle regulation of histone H1 kinase activity associated with the adenoviral protein E1A

Giordano, A., Lee, J. H., Scheppler, J. A., Herrmann, C., Harlow, E., Deuschle, U., Beach, D., Franza, B. R. (September 1991) Cell cycle regulation of histone H1 kinase activity associated with the adenoviral protein E1A. Science, 253 (5025). pp. 1271-5. ISSN 0036-8075 (Print)0036-8075 (Linking)

URL: http://www.ncbi.nlm.nih.gov/pubmed/1653969
DOI: 10.1126/science.1653969

Abstract

Several cellular proteins form stable complexes with the proteins encoded by the adenovirus early region 1A (E1A) gene in extracts derived from adenovirus infected or transformed cells. Two of the cellular proteins that bind to E1A have been identified; one, a 105-kilodalton protein (pRb), is the product of the retinoblastoma gene, and the other, a 60-kilodalton protein, is a human cyclin A. Two other proteins that bind E1A have now been shown to be related to p34cdc2. This E1A complex displayed histone H1-specific kinase activity; the kinase activity was modulated during the cell division cycle, and association of pRb with E1A apparently was not required for this activity.

Item Type: Paper
Uncontrolled Keywords: Adenovirus Early Proteins Adenoviruses, Human/*genetics CDC2 Protein Kinase/*metabolism *Cell Cycle Cell Line Cell Transformation, Neoplastic DNA-Binding Proteins/metabolism HeLa Cells/cytology/physiology Humans Oncogene Proteins, Viral/genetics/*metabolism Protamine Kinase/*metabolism Protein Binding Recombination, Genetic
Subjects: organism description > virus > adenovirus
organs, tissues, organelles, cell types and functions > cell types and functions > cell functions > cell cycle
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > histone
CSHL Authors:
Communities: CSHL labs > Beach lab
Depositing User: Matt Covey
Date: 13 September 1991
Date Deposited: 13 Jan 2016 20:24
Last Modified: 13 Jan 2016 20:24
Related URLs:
URI: https://repository.cshl.edu/id/eprint/32048

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