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CK2 phosphorylation inactivates DNA binding by the papillomavirus E1 and E2 proteins

Stephen Schuck1, Cristian Ruse, Arne Stenlund

  • 1Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, USA.

Journal of Virology
|May 3, 2013
PubMed

Insights

Protein kinase CK2 phosphorylation regulates bovine papillomavirus E1 and E2 protein DNA binding. This phosphorylation controls viral replication, with E2 acting as a negative regulator during latent replication.

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • Papillomavirus life cycles are complex and not fully understood.
  • Viral E1 and E2 proteins are crucial for transcription and DNA replication.
  • Regulation of E1 and E2 protein activity remains largely unclear.

Purpose of the Study:

  • To investigate the role of protein kinase CK2 in regulating bovine papillomavirus (BPV) E1 and E2 protein functions.
  • To determine how CK2 phosphorylation affects the DNA binding activities of BPV E1 and E2 proteins.
  • To elucidate the impact of CK2-mediated phosphorylation on viral DNA replication.

Main Methods:

  • Investigated the effect of CK2 phosphorylation on BPV E1 and E2 protein DNA binding.
  • Analyzed phosphorylation sites in E1 and E2 proteins using mutational analysis.
  • Assessed the impact of mutations on viral DNA replication during latent and vegetative phases.

Main Results:

  • CK2 phosphorylation of BPV E1 and E2 proteins alters their DNA binding activity.
  • Phosphorylation of BPV E1's N-terminal domain leads to loss of DNA binding, conserved in human papillomavirus (HPV) E1.
  • CK2 phosphorylation of BPV E2's hinge region also reduces DNA binding; mutations here increase latent replication.
  • N-terminal E1 phosphorylation sites are not essential for latent replication but may be for vegetative replication.

Conclusions:

  • CK2 phosphorylation is a key regulatory mechanism for BPV E1 and E2 protein biochemical activities.
  • CK2 phosphorylation of E2 acts as a negative regulator of viral DNA replication during latency.
  • E1 N-terminal phosphorylation likely plays a role in vegetative replication, potentially reversed by caspase 3 cleavage.

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