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Virology. 2008 Apr 25;374(1):1-10. doi: 10.1016/j.virol.2007.11.023. Epub 2008 Jan 22.

Substrate specificity of the herpes simplex virus type 2 UL13 protein kinase.

Author information

1
Department of Molecular Microbiology and Immunology, Saint Louis University School of Medicine, 1100 South Grand Blvd., St. Louis, MO 63104, USA. canogl@slu.edu

Abstract

The UL13 protein kinase is conserved among many herpesviruses but HSV-2 UL13 specificity is not known. Here, we found that HSV-2 UL13 is a phosphoprotein that autophosphorylates, and that serines within ERK and Cdc2 motifs were important for autophosphorylation but not for UL13 phosphorylation of exogenous substrates. HSV-2 UL13 phosphorylated a peptide also recognized by ERK and Cdc2. However, mutation of substrate residues critical for Cdc2 or Erk phosphorylation did not alter HSV-2 UL13 phosphorylation of the peptide, and HSV-2 UL13 did not phosphorylate standard Cdc2 or Erk peptide substrates. Mutation of prolines surrounding the peptide phosphoacceptor site reduced phosphorylation by HSV-2 UL13, and a peptide containing serine-proline amid alanines and glycines was phosphorylated. Thus, HSV-2 UL13 does not mimic ERK or Cdc2 substrate recognition and its minimal recognition motif can be serine-proline. This motif's simplicity indicates that distal sequence or protein structure contributes to HSV-2 UL13 substrate specificity.

PMID:
18207213
PMCID:
PMC2396491
DOI:
10.1016/j.virol.2007.11.023
[Indexed for MEDLINE]
Free PMC Article

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