title: Substrate specificity of the herpes simplex virus type 2 UL13 protein kinase.
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.
authors.affiliation: Department of Molecular Microbiology and Immunology, Saint Louis University School of Medicine, 1100 South Grand Blvd., St. Louis, MO 63104, USA. canogl@slu.edu
authors.forename: Gina L
authors.initials: GL
authors.lastname: Cano-Monreal
authors.forename: John E
authors.initials: JE
authors.lastname: Tavis
authors.forename: Lynda A
authors.initials: LA
authors.lastname: Morrison
mesh_terms: D018258:Herpesvirus 2, Human / Q000201:enzymology*; D010455:Peptides / Q000378:metabolism; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000737:chemistry / Q000378:metabolism*; D012694:Serine / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D010455:Peptides; D010750:Phosphoproteins; D012694:Serine; D011494:Protein Kinases; C082380:UL13 protein, Simplexvirus