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Cell Cycle Stage-specific Phosphorylation of the Epstein-Barr Virus Immortalization Protein EBNA-LP

Overview
Journal J Virol
Date 1996 Nov 1
PMID 8892911
Citations 27
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Abstract

EBNA-LP is a viral nuclear oncoprotein implicated in the immortalization of B lymphocytes by Epstein-Barr virus. An analysis of EBNA-LP migration on polyacrylamide gels was performed with protein derived from the X50-7 lymphoblastoid cell line blocked by hydroxyurea or aphidicolin at the G1/S phase of the cell cycle or by nocodazole at the G2/M phase. More slowly migrating species of EBNA-LP were detected in G2/M phase-arrested cell extracts. Release from nocodazole G2/M block or treatment with phosphatase caused the more slowly migrating species of EBNA-LP to disappear. Analyses of 32PO(4)(3-)-labeled EBNA-LP protein immunoprecipitated from the drug-synchronized cells showed that phosphorylated EBNA-LP was present throughout the cell cycle but that phosphorylation increased in G2 and was maximal at G2/M. Phosphoamino acid analysis revealed that all phosphorylation was on serine residues only. The ability of EBNA-LP to be phosphorylated by p34(cdc2) kinase and casein kinase II exclusively on serines implicates these enzymes as being potentially involved in EBNA-LP phosphorylation.

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References
1.
Bousset K, Oelgeschlager M, Henriksson M, Schreek S, Burkhardt H, Litchfield D . Regulation of transcription factors c-Myc, Max, and c-Myb by casein kinase II. Cell Mol Biol Res. 1994; 40(5-6):501-11. View

2.
Kitay M, Rowe D . Protein-protein interactions between Epstein-Barr virus nuclear antigen-LP and cellular gene products: binding of 70-kilodalton heat shock proteins. Virology. 1996; 220(1):91-9. DOI: 10.1006/viro.1996.0289. View

3.
Inman G, Farrell P . Epstein-Barr virus EBNA-LP and transcription regulation properties of pRB, p107 and p53 in transfection assays. J Gen Virol. 1995; 76 ( Pt 9):2141-9. DOI: 10.1099/0022-1317-76-9-2141. View

4.
Wilson G, Miller G . Recovery of Epstein-Barr virus from nonproducer neonatal human lymphoid cell transformants. Virology. 1979; 95(2):351-8. DOI: 10.1016/0042-6822(79)90490-2. View

5.
Rawlins D, Milman G, Hayward S, Hayward G . Sequence-specific DNA binding of the Epstein-Barr virus nuclear antigen (EBNA-1) to clustered sites in the plasmid maintenance region. Cell. 1985; 42(3):859-68. DOI: 10.1016/0092-8674(85)90282-x. View