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.
Keywords:
DNA replication; E1 protein; Kinase CK2; Papillomavirus; Protein phosphorylation.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Bovine papillomavirus 1 / chemistry
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Bovine papillomavirus 1 / genetics
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Bovine papillomavirus 1 / metabolism*
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Casein Kinase II / genetics
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Casein Kinase II / metabolism*
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Cattle
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Cattle Diseases / enzymology*
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Cattle Diseases / genetics
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Cattle Diseases / virology
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Cell Nucleus / virology
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DNA-Binding Proteins / chemistry*
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism*
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Molecular Sequence Data
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Nuclear Localization Signals / chemistry
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Nuclear Localization Signals / genetics
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Nuclear Localization Signals / metabolism*
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Papillomavirus Infections / enzymology
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Papillomavirus Infections / genetics
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Papillomavirus Infections / veterinary*
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Papillomavirus Infections / virology
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Phosphorylation
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Protein Transport
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Viral Proteins / chemistry*
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Viral Proteins / genetics
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Viral Proteins / metabolism*
Substances
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DNA-Binding Proteins
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E1 protein, Bovine papillomavirus
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Nuclear Localization Signals
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Viral Proteins
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Casein Kinase II