Modulation of Bovine Papillomavirus DNA Replication by Phosphorylation of the Viral E1 Protein

E1 is the DNA replication origin recognition protein for bovine papillomavirus (BPV), and it carries out enzymatic functions required for initiation of viral DNA replication. Cellular mechanisms likely play a role in regulating BPV DNA replication. We are investigating the role of phosphorylation of...

Full description

Saved in:
Bibliographic Details
Published in:Virology (New York, N.Y.) N.Y.), 1997-02, Vol.228 (1), p.1-10
Main Authors: ZANARDI, THOMAS A, STANLEY, CHRISTINE M, SAVILLE, BRADLEY M, SPACEK, SUSAN M, LENTZ, MICHAEL R
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - genetics
Adenosine Triphosphatases - metabolism
ADN
Alanine
Animals
Binding Sites
Bovine papillomavirus
Bovine papillomavirus 1
Bovine papillomavirus 1 - genetics
Bovine papillomavirus 1 - physiology
Cattle
Cell Line
CHO Cells
Cricetinae
DNA Helicases
DNA Replication
DNA, Viral - biosynthesis
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
FOSFORILACION
Genome, Viral
Glutamic Acid
Mice
Mutagenesis
PAPILLOMAVIRUS BOVIN
PHOSPHORYLATION
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Replication Origin
Serine
Spodoptera - cytology
Tumor Cells, Cultured
Viral Proteins - genetics
Viral Proteins - metabolism
VIRUS DEL PAPILOMA BOVINO
Virus Replication
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:E1 is the DNA replication origin recognition protein for bovine papillomavirus (BPV), and it carries out enzymatic functions required for initiation of viral DNA replication. Cellular mechanisms likely play a role in regulating BPV DNA replication. We are investigating the role of phosphorylation of E1 on viral replicationin vivoand on E1 activityin vitro.Serine 109 is a phosphoacceptorin vivoand is targeted by protein kinase A and protein kinase Cin vitro.A viral genome carrying a serine 109 to alanine mutation replicates more efficiently than wild-typein vivoin a transient replication assay. Furthermore, purified mutant protein, while having wild-type levels of ATPase activity, is able to bind more origin-containing DNA than wild-type E1. Phosphorylation therefore appears to play a selective role in modulating a specific E1 function during viral DNA replication.
ISSN:0042-6822
1096-0341
DOI:10.1006/viro.1996.8375