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Phosphorylation of herpes simplex virus type 1 Us11 protein is independent of viral genome expression
Author(s) -
Simonin Denis,
Diaz JeanJacques,
Kindbeiter Karine,
Pernas Patrick,
Madjar JeanJacques
Publication year - 1995
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.11501601216
Subject(s) - biology , phosphorylation , herpes simplex virus , autophagy related protein 13 , microbiology and biotechnology , protein kinase a , gene , gps2 , protein phosphorylation , akt1s1 , virology , biochemistry , hspa2 , peptide sequence , virus
The Us11 protein is a true late gene product of herpes simplex virus type 1 (HSV‐1), whose exact function is unknown but which exhibits RNA‐binding properties and which is phosphorylated on serine residues. In order to determine whether the Us11 protein is phosphorylated by cellular kinase(s) or by virally encoded kinase(s), the Us11 gene has been cloned and transiently expressed in HeLa cells. In addition, HeLa‐derived cell lines have been selected for their ability to express Us11 protein constitutively. 32 P‐Labeling and analysis by two‐dimensional electrophoresis of transiently and constitutively expressed Us11 protein demonstrated that, indeed, multiple phosphorylation of the protein occurs in absence of HSV‐1 genome expression, indicating that the protein behaves as a natural substrate for cellular kinase(s). In addition, a sequence heterogeneity of the Us11 protein, due to a difference in the number of SPREPR repeats, has been characterized between different strains of HSV‐1.