Phosphorylation of bovine papillomavirus E1 by the protein kinase CK2 near the nuclear localization signal does not influence subcellular distribution of the protein in dividing cells
Document Type
Article
Publication Date
1-1-2016
Abstract
The bovine papillomavirus E1 helicase is essential for viral replication. In dividing cells, DNA replication maintains, but does not increase, the viral genome copy number. Replication is limited by low E1 expression and an E1 nucleocytoplasmic shuttling mechanism. Shuttling is controlled in part by phosphorylation of E1 by cellular kinases. Here we investigate conserved sites for phosphorylation by kinase CK2 within the E1 nuclear localization signal. When these CK2 sites are mutated to either alanine or aspartic acid, no change in replication phenotype is observed, and there is no effect on the subcellular distribution of E1, which remains primarily nuclear. This demonstrates that phosphorylation of E1 by CK2 at these sites is not a factor in regulating viral DNA replication in dividing cells.
Publication Title
Archives of Virology
Volume
161
Issue
1
First Page
165
Last Page
169
Digital Object Identifier (DOI)
10.1007/s00705-015-2641-6
PubMed ID
26467928
ISSN
03048608
Citation Information
Lentz, & Shideler, T. (2015). Phosphorylation of bovine papillomavirus E1 by the protein kinase CK2 near the nuclear localization signal does not influence subcellular distribution of the protein in dividing cells. Archives of Virology, 161(1), 165–169. https://doi.org/10.1007/s00705-015-2641-6